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380  structures 1468  species 0  interactions 105778  sequences 2798  architectures

Family: PH (PF00169)

Summary: PH domain

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

This is the Wikipedia entry entitled "Pleckstrin homology domain". More...

Pleckstrin homology domain Edit Wikipedia article

1bwn opm.png
PH domain of tyrosine-protein kinase BTK
Identifiers
SymbolPH
PfamPF00169
Pfam clanCL0266
InterProIPR001849
SMARTPH
PROSITEPDOC50003
SCOPe1dyn / SUPFAM
OPM superfamily49
OPM protein1pls
CDDcd00821

Pleckstrin homology domain (PH domain) or (PHIP) is a protein domain of approximately 120 amino acids that occurs in a wide range of proteins involved in intracellular signaling or as constituents of the cytoskeleton.[1][2][3][4][5][6][7]

This domain can bind phosphatidylinositol lipids within biological membranes (such as phosphatidylinositol (3,4,5)-trisphosphate and phosphatidylinositol (4,5)-bisphosphate),[8] and proteins such as the βγ-subunits of heterotrimeric G proteins,[9] and protein kinase C.[10] Through these interactions, PH domains play a role in recruiting proteins to different membranes, thus targeting them to appropriate cellular compartments or enabling them to interact with other components of the signal transduction pathways.

Lipid binding specificity

Individual PH domains possess specificities for phosphoinositides phosphorylated at different sites within the inositol ring, e.g., some bind phosphatidylinositol (4,5)-bisphosphate but not phosphatidylinositol (3,4,5)-trisphosphate or phosphatidylinositol (3,4)-bisphosphate, while others may possess the requisite affinity. This is important because it makes the recruitment of different PH domain containing proteins sensitive to the activities of enzymes that either phosphorylate or dephosphorylate these sites on the inositol ring, such as phosphoinositide 3-kinase or PTEN, respectively. Thus, such enzymes exert a part of their effect on cell function by modulating the localization of downstream signaling proteins that possess PH domains that are capable of binding their phospholipid products.

Structure

The 3D structure of several PH domains has been determined.[11] All known cases have a common structure consisting of two perpendicular anti-parallel beta sheets, followed by a C-terminal amphipathic helix. The loops connecting the beta-strands differ greatly in length, making the PH domain relatively difficult to detect while providing the source of the domain's specificity. The only conserved residue among PH domains is a single tryptophan located within the alpha helix that serves to nucleate the core of the domain.

Proteins containing PH domain

PH domains can be found in many different proteins, such as OSBP or ARF. Recruitment to the Golgi in this case is dependent on both PtdIns and ARF. A large number of PH domains have poor affinity for phosphoinositides and are hypothesized to function as protein binding domains. A Genome-wide look in Saccharomyces cerevisiae showed that most of the 33 yeast PH domains are indeed promiscuous in binding to phosphoinositides, while only one (Num1-PH) behaved highly specific .[12] Proteins reported to contain PH domains belong to the following families:

  • Pleckstrin, the protein where this domain was first detected, is the major substrate of protein kinase C in platelets. Pleckstrin contains two PH domains. ARAP proteins contain five PH domains.
  • Ser/Thr protein kinases such as the Akt/Rac family, the beta-adrenergic receptor kinases, the mu isoform of PKC and the trypanosomal NrkA family.
  • Tyrosine protein kinases belonging to the Btk/Itk/Tec subfamily.
  • Insulin receptor substrate 1 (IRS-1).
  • Regulators of small G-proteins: 64 RhoGEFs of the Dbl-like family. [13], and several GTPase activating proteins like ABR, BCR or ARAP proteins.
  • Cytoskeletal proteins such as dynamin (see InterProIPR001401), Caenorhabditis elegans kinesin-like protein unc-104 (see InterProIPR001752), spectrin beta-chain, syntrophin (2 PH domains), and S. cerevisiae nuclear migration protein NUM1.
  • Oxysterol-binding proteins OSBP, S. cerevisiae OSH1 and YHR073w.
  • Ceramide kinase, a lipid kinase that phosphorylates ceramides to ceramide-1-phosphate.
  • G protein receptor kinases 2 (GRK2) subfamily 2: GRK2 and GRK3 [14]

Sugiura M, Kono K, Liu H, Shimizugawa T, Minekura H, Spiegel S, Kohama T (June 2002). "Ceramide kinase, a novel lipid kinase. Molecular cloning and functional characterization". The Journal of Biological Chemistry. 277 (26): 23294–300. doi:10.1074/jbc.M201535200. PMID 11956206.</ref>

Subfamilies

Examples

Human genes encoding proteins containing this domain include:

See also

References

  1. ^ Mayer BJ, Ren R, Clark KL, Baltimore D (May 1993). "A putative modular domain present in diverse signaling proteins". Cell. 73 (4): 629–30. doi:10.1016/0092-8674(93)90244-K. PMID 8500161.
  2. ^ Haslam RJ, Koide HB, Hemmings BA (May 1993). "Pleckstrin domain homology". Nature. 363 (6427): 309–10. doi:10.1038/363309b0. PMID 8497315.
  3. ^ Musacchio A, Gibson T, Rice P, Thompson J, Saraste M (September 1993). "The PH domain: a common piece in the structural patchwork of signalling proteins". Trends in Biochemical Sciences. 18 (9): 343–8. doi:10.1016/0968-0004(93)90071-T. PMID 8236453.
  4. ^ Gibson TJ, Hyvönen M, Musacchio A, Saraste M, Birney E (September 1994). "PH domain: the first anniversary". Trends in Biochemical Sciences. 19 (9): 349–53. doi:10.1016/0968-0004(94)90108-2. PMID 7985225.
  5. ^ Pawson T (February 1995). "Protein modules and signalling networks". Nature. 373 (6515): 573–80. doi:10.1038/373573a0. PMID 7531822.
  6. ^ Ingley E, Hemmings BA (December 1994). "Pleckstrin homology (PH) domains in signal transduction". Journal of Cellular Biochemistry. 56 (4): 436–43. doi:10.1002/jcb.240560403. PMID 7890802.
  7. ^ Saraste M, Hyvönen M (June 1995). "Pleckstrin homology domains: a fact file". Current Opinion in Structural Biology. 5 (3): 403–8. doi:10.1016/0959-440X(95)80104-9. PMID 7583640.
  8. ^ Wang DS, Shaw G (December 1995). "The association of the C-terminal region of beta I sigma II spectrin to brain membranes is mediated by a PH domain, does not require membrane proteins, and coincides with a inositol-1,4,5 triphosphate binding site". Biochemical and Biophysical Research Communications. 217 (2): 608–15. doi:10.1006/bbrc.1995.2818. PMID 7503742.
  9. ^ Wang DS, Shaw R, Winkelmann JC, Shaw G (August 1994). "Binding of PH domains of beta-adrenergic receptor kinase and beta-spectrin to WD40/beta-transducin repeat containing regions of the beta-subunit of trimeric G-proteins". Biochemical and Biophysical Research Communications. 203 (1): 29–35. doi:10.1006/bbrc.1994.2144. PMID 8074669.
  10. ^ Yao L, Kawakami Y, Kawakami T (September 1994). "The pleckstrin homology domain of Bruton tyrosine kinase interacts with protein kinase C". Proceedings of the National Academy of Sciences of the United States of America. 91 (19): 9175–9. doi:10.1073/pnas.91.19.9175. PMC 44770. PMID 7522330.
  11. ^ Riddihough G (November 1994). "More meanders and sandwiches". Nature Structural Biology. 1 (11): 755–7. doi:10.1038/nsb1194-755. PMID 7634082.
  12. ^ Yu JW, Mendrola JM, Audhya A, Singh S, Keleti D, DeWald DB, Murray D, Emr SD, Lemmon MA (March 2004). "Genome-wide analysis of membrane targeting by S. cerevisiae pleckstrin homology domains". Molecular Cell. 13 (5): 677–88. doi:10.1016/S1097-2765(04)00083-8. PMID 15023338.
  13. ^ Fort P, Blangy A (June 2017). "The Evolutionary Landscape of Dbl-Like RhoGEF Families: Adapting Eukaryotic Cells to Environmental Signals". Genome Biol Evol. 9 (6): 1471–1486. doi:10.1093/gbe/evx100. PMC 5499878. PMID 28541439.
  14. ^ Komolov KE, Benovic JL (January 2018). "G protein-coupled receptor kinases: Past, present and future". Cellular Signalling. 41: 17–24. doi:10.1016/j.cellsig.2017.07.004. PMC 5722692. PMID 28711719.

External links

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

PH domain Provide feedback

PH stands for pleckstrin homology.

Literature references

  1. Gibson TJ, Hyvonen M, Musacchio A, Saraste M, Birney E; , Trends Biochem Sci 1994;19:349-353.: PH domain: the first anniversary. PUBMED:7985225 EPMC:7985225


Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR001849

Pleckstrin homology (PH) domains are small modular domains that occur in a large variety of proteins. The domains can bind phosphatidylinositol within biological membranes and proteins such as the beta/gamma subunits of heterotrimeric G proteins [ PUBMED:8074669 ] and protein kinase C [ PUBMED:7522330 ]. Through these interactions, PH domains play a role in recruiting proteins to different membranes, thus targeting them to appropriate cellular compartments or enabling them to interact with other components of the signal transduction pathways.

PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.

The 3D structure of several PH domains has been determined [ PUBMED:7634082 ]. All known cases have a common structure consisting of two perpendicular anti-parallel beta sheets, followed by a C-terminal amphipathic helix. The loops connecting the beta-strands differ greatly in length, making the PH domain relatively difficult to detect. There are no totally invariant residues within the PH domain.

Proteins reported to contain one more PH domains belong to the following families:

  • Pleckstrin, the protein where this domain was first detected, is the major substrate of protein kinase C in platelets. Pleckstrin is one of the rare proteins to contains two PH domains.
  • Ser/Thr protein kinases such as the Akt/Rac family, the beta-adrenergic receptor kinases, the mu isoform of PKC and the trypanosomal NrkA family.
  • Tyrosine protein kinases belonging to the Btk/Itk/Tec subfamily.
  • Insulin Receptor Substrate 1 (IRS-1).
  • Regulators of small G-proteins like guanine nucleotide releasing factor GNRP (Ras-GRF) (which contains 2 PH domains), guanine nucleotide exchange proteins like vav, dbl, SoS and Saccharomyces cerevisiae CDC24, GTPase activating proteins like rasGAP and BEM2/IPL2, and the human break point cluster protein bcr.
  • Cytoskeletal proteins such as dynamin (see INTERPRO ), Caenorhabditis elegans kinesin-like protein unc-104 (see INTERPRO ), spectrin beta-chain, syntrophin (2 PH domains) and S. cerevisiae nuclear migration protein NUM1.
  • Mammalian phosphatidylinositol-specific phospholipase C (PI-PLC) (see INTERPRO ) isoforms gamma and delta. Isoform gamma contains two PH domains, the second one is split into two parts separated by about 400 residues.
  • Oxysterol binding proteins OSBP, S. cerevisiae OSH1 and YHR073w.
  • Mouse protein citron, a putative rho/rac effector that binds to the GTP-bound forms of rho and rac.
  • Several S. cerevisiae proteins involved in cell cycle regulation and bud formation like BEM2, BEM3, BUD4 and the BEM1-binding proteins BOI2 (BEB1) and BOI1 (BOB1).
  • C. elegans protein MIG-10.
  • C. elegans hypothetical proteins C04D8.1, K06H7.4 and ZK632.12.
  • S. cerevisiae hypothetical proteins YBR129c and YHR155w.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(111)
Full
(105778)
Representative proteomes UniProt
(186167)
RP15
(12384)
RP35
(34915)
RP55
(88888)
RP75
(122339)
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Format an alignment

  Seed
(111)
Full
(105778)
Representative proteomes UniProt
(186167)
RP15
(12384)
RP35
(34915)
RP55
(88888)
RP75
(122339)
Alignment:
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(111)
Full
(105778)
Representative proteomes UniProt
(186167)
RP15
(12384)
RP35
(34915)
RP55
(88888)
RP75
(122339)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download  

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: SMART
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: SMART
Number in seed: 111
Number in full: 105778
Average length of the domain: 104.60 aa
Average identity of full alignment: 17 %
Average coverage of the sequence by the domain: 12.58 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 57096847 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 25.1 25.1
Trusted cut-off 25.1 25.1
Noise cut-off 25.0 25.0
Model length: 105
Family (HMM) version: 31
Download: download the raw HMM for this family

Species distribution

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Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the PH domain has been found. There are 380 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
A0A0A0MPH2 View 3D Structure Click here
A0A0A0MPV6 View 3D Structure Click here
A0A0A0MPV6 View 3D Structure Click here
A0A0B4JCZ0 View 3D Structure Click here
A0A0B4LHY5 View 3D Structure Click here
A0A0G2JTI5 View 3D Structure Click here
A0A0G2JTR4 View 3D Structure Click here
A0A0G2JTT7 View 3D Structure Click here
A0A0G2JV16 View 3D Structure Click here
A0A0G2JW65 View 3D Structure Click here
A0A0G2JWC7 View 3D Structure Click here
A0A0G2JXN8 View 3D Structure Click here
A0A0G2JZD5 View 3D Structure Click here
A0A0G2K0A0 View 3D Structure Click here
A0A0G2K134 View 3D Structure Click here
A0A0G2K1A8 View 3D Structure Click here
A0A0G2K1A8 View 3D Structure Click here
A0A0G2K1P8 View 3D Structure Click here
A0A0G2K1Z2 View 3D Structure Click here
A0A0G2K1Z6 View 3D Structure Click here
A0A0G2K246 View 3D Structure Click here
A0A0G2K246 View 3D Structure Click here
A0A0G2K2U9 View 3D Structure Click here
A0A0G2K5N8 View 3D Structure Click here
A0A0G2K6Z8 View 3D Structure Click here
A0A0G2K7I9 View 3D Structure Click here
A0A0G2K7I9 View 3D Structure Click here
A0A0G2K7I9 View 3D Structure Click here
A0A0G2K7L6 View 3D Structure Click here
A0A0G2K7L6 View 3D Structure Click here
A0A0G2K7U5 View 3D Structure Click here
A0A0G2K808 View 3D Structure Click here
A0A0G2K847 View 3D Structure Click here
A0A0G2KA11 View 3D Structure Click here
A0A0G2KA94 View 3D Structure Click here
A0A0G2KB72 View 3D Structure Click here
A0A0G2KMB1 View 3D Structure Click here
A0A0G2KQU1 View 3D Structure Click here
A0A0G2KXI9 View 3D Structure Click here
A0A0H2UKT8 View 3D Structure Click here
A0A0N7KGY7 View 3D Structure Click here
A0A0R0EFI1 View 3D Structure Click here
A0A0R0FEV9 View 3D Structure Click here
A0A0R0KCB2 View 3D Structure Click here
A0A0R4I9G1 View 3D Structure Click here
A0A0R4I9G1 View 3D Structure Click here
A0A0R4I9X7 View 3D Structure Click here
A0A0R4IAC2 View 3D Structure Click here
A0A0R4IB99 View 3D Structure Click here
A0A0R4IB99 View 3D Structure Click here
A0A0R4IDU6 View 3D Structure Click here
A0A0R4IE40 View 3D Structure Click here
A0A0R4IE40 View 3D Structure Click here
A0A0R4IE78 View 3D Structure Click here
A0A0R4IG21 View 3D Structure Click here
A0A0R4IG21 View 3D Structure Click here
A0A0R4IG72 View 3D Structure Click here
A0A0R4IG72 View 3D Structure Click here
A0A0R4IGI8 View 3D Structure Click here
A0A0R4IH20 View 3D Structure Click here
A0A0R4IIR1 View 3D Structure Click here
A0A0R4IKQ9 View 3D Structure Click here
A0A0R4ILP5 View 3D Structure Click here
A0A0R4ILP5 View 3D Structure Click here
A0A0R4IM47 View 3D Structure Click here
A0A0R4IP09 View 3D Structure Click here
A0A0R4IPM9 View 3D Structure Click here
A0A0R4IQ17 View 3D Structure Click here
A0A0R4IQ50 View 3D Structure Click here
A0A0R4IQD5 View 3D Structure Click here
A0A0R4IRL3 View 3D Structure Click here
A0A0R4IRU6 View 3D Structure Click here
A0A0R4IV74 View 3D Structure Click here
A0A0R4IY09 View 3D Structure Click here
A0A140LH27 View 3D Structure Click here
A0A143ZWC2 View 3D Structure Click here
A0A1D5NSU5 View 3D Structure Click here
A0A1D6F313 View 3D Structure Click here
A0A1D6F3P8 View 3D Structure Click here
A0A1D6FHM8 View 3D Structure Click here
A0A1D6GKP6 View 3D Structure Click here
A0A1D6HJQ5 View 3D Structure Click here
A0A1D6I8A5 View 3D Structure Click here
A0A1D6ILZ1 View 3D Structure Click here
A0A1D6IYX9 View 3D Structure Click here
A0A1D6JWD7 View 3D Structure Click here
A0A1D6K3H5 View 3D Structure Click here
A0A1D6KPH4 View 3D Structure Click here
A0A1D6KSV2 View 3D Structure Click here
A0A1D6LJA1 View 3D Structure Click here
A0A1D6M211 View 3D Structure Click here
A0A1D6MEM7 View 3D Structure Click here
A0A1D6NRA8 View 3D Structure Click here
A0A1D6NXB3 View 3D Structure Click here
A0A1D6PEF4 View 3D Structure Click here
A0A1D6PYH0 View 3D Structure Click here
A0A1D6Q5I5 View 3D Structure Click here
A0A1D8PD21 View 3D Structure Click here
A0A1D8PD25 View 3D Structure Click here
A0A1D8PE79 View 3D Structure Click here
A0A1D8PF97 View 3D Structure Click here
A0A1D8PLJ2 View 3D Structure Click here
A0A1D8PNH1 View 3D Structure Click here
A0A1D8PNH1 View 3D Structure Click here
A0A1D8PPT0 View 3D Structure Click here
A0A1D8PRW9 View 3D Structure Click here
A0A286Y8A3 View 3D Structure Click here
A0A286Y8W8 View 3D Structure Click here
A0A286Y917 View 3D Structure Click here
A0A286Y9S9 View 3D Structure Click here
A0A2R8PWA9 View 3D Structure Click here
A0A2R8PZF7 View 3D Structure Click here
A0A2R8Q0A4 View 3D Structure Click here
A0A2R8Q0B2 View 3D Structure Click here
A0A2R8Q0B2 View 3D Structure Click here
A0A2R8Q0N0 View 3D Structure Click here
A0A2R8Q4K6 View 3D Structure Click here
A0A2R8Q548 View 3D Structure Click here
A0A2R8Q628 View 3D Structure Click here
A0A2R8Q6D5 View 3D Structure Click here
A0A2R8QB47 View 3D Structure Click here
A0A2R8QCF3 View 3D Structure Click here
A0A2R8QCJ5 View 3D Structure Click here
A0A2R8QD21 View 3D Structure Click here
A0A2R8QER8 View 3D Structure Click here
A0A2R8QER8 View 3D Structure Click here
A0A2R8QFM9 View 3D Structure Click here
A0A2R8QFY5 View 3D Structure Click here
A0A2R8QHS4 View 3D Structure Click here
A0A2R8QHS4 View 3D Structure Click here
A0A2R8QIU8 View 3D Structure Click here
A0A2R8QJT7 View 3D Structure Click here
A0A2R8QLB0 View 3D Structure Click here
A0A2R8QM99 View 3D Structure Click here
A0A2R8QPA9 View 3D Structure Click here
A0A2R8QPB8 View 3D Structure Click here
A0A2R8QRR7 View 3D Structure Click here
A0A2R8QS69 View 3D Structure Click here
A0A2R8QT19 View 3D Structure Click here
A0A2R8QUA5 View 3D Structure Click here
A0A2R8QUR4 View 3D Structure Click here
A0A2R8QUR4 View 3D Structure Click here
A0A2R8RHL8 View 3D Structure Click here
A0A2R8RSL7 View 3D Structure Click here
A0A2R8RU01 View 3D Structure Click here
A0A2R8RW52 View 3D Structure Click here
A0A2R8RW84 View 3D Structure Click here
A0A2R8RXH3 View 3D Structure Click here
A0A2R9YJH0 View 3D Structure Click here
A0JMN8 View 3D Structure Click here
A1A4S6 View 3D Structure Click here
A1A535 View 3D Structure Click here
A1L1F5 View 3D Structure Click here
A1L390 View 3D Structure Click here
A1Z714 View 3D Structure Click here
A1Z7A6 View 3D Structure Click here
A1Z814 View 3D Structure Click here
A1ZAJ2 View 3D Structure Click here
A2A8Z1 View 3D Structure Click here
A2A9K7 View 3D Structure Click here
A2AB59 View 3D Structure Click here
A2AF47 View 3D Structure Click here
A2AR50 View 3D Structure Click here
A2BEG1 View 3D Structure Click here
A2BFQ2 View 3D Structure Click here
A2BGE8 View 3D Structure Click here
A2BGK1 View 3D Structure Click here
A2BI20 View 3D Structure Click here
A2BID5 View 3D Structure Click here
A2CEA7 View 3D Structure Click here
A2RUZ0 View 3D Structure Click here
A4HTY4 View 3D Structure Click here
A4I5B1 View 3D Structure Click here
A4I7C4 View 3D Structure Click here
A4I7Z6 View 3D Structure Click here
A4I960 View 3D Structure Click here
A4IC37 View 3D Structure Click here
A4IDC2 View 3D Structure Click here
A4IE45 View 3D Structure Click here
A4IG55 View 3D Structure Click here
A5D6R3 View 3D Structure Click here
A5PKW4 View 3D Structure Click here
A6NEE1 View 3D Structure Click here
A6NI28 View 3D Structure Click here
A8JQ65 View 3D Structure Click here
A9C3U0 View 3D Structure Click here
A9C3U0 View 3D Structure Click here
B0R034 View 3D Structure Click here
B0S4U0 View 3D Structure Click here
B0S541 View 3D Structure Click here
B0S541 View 3D Structure Click here
B0S5M3 View 3D Structure Click here
B0S6C8 View 3D Structure Click here
B0S7L9 View 3D Structure Click here
B0S8J8 View 3D Structure Click here
B0UXH6 View 3D Structure Click here
B0V1J1 View 3D Structure Click here
B1AVH7 View 3D Structure Click here
B1WBU8 View 3D Structure Click here
B1WBV4 View 3D Structure Click here
B2GUW2 View 3D Structure Click here
B2GVB9 View 3D Structure Click here
B2RPU2 View 3D Structure Click here
B2RQE8 View 3D Structure Click here
B3DLH5 View 3D Structure Click here
B3DLH5 View 3D Structure Click here
B4F779 View 3D Structure Click here
B4F791 View 3D Structure Click here
B4G051 View 3D Structure Click here
B5DEJ9 View 3D Structure Click here
B5DF74 View 3D Structure Click here
B5DFA1 View 3D Structure Click here
B5DFL0 View 3D Structure Click here
B6RSP1 View 3D Structure Click here
B6T5A7 View 3D Structure Click here
B6UCM9 View 3D Structure Click here
B8JI51 View 3D Structure Click here
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