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26  structures 1390  species 0  interactions 241615  sequences 13775  architectures

Family: PPR (PF01535)

Summary: PPR repeat

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 "Pentatricopeptide repeat". More...

Pentatricopeptide repeat Edit Wikipedia article

Pentatricopeptide repeat
Identifiers
SymbolPPR
PfamPF01535
Pfam clanCL0020
InterProIPR002885
PROSITEPS51375

The pentatricopeptide repeat (PPR) is a 35-amino acid sequence motif. Pentatricopeptide-repeat-containing proteins are a family of proteins commonly found in the plant kingdom. They are distinguished by the presence of tandem degenerate PPR motifs[1] and by the relative lack of introns in the genes coding for them.[2]

Approximately 450 such proteins have been identified in the Arabidopsis genome, and another 477 in the rice genome.[3] Despite the large size of the protein family, genetic data suggest that there is little or no redundancy of function between the PPR proteins in Arabidopsis.[2]

The purpose of PPR proteins is currently under dispute. It has been shown that a good deal of those in Arabidopsis interact (often essentially) with mitochondria and other organelles[2] and that they are possibly involved in RNA editing.[4] However many trans proteins are required for this editing to occur and research continues to look at which proteins are needed.[5]

The structure of the PPR has been resolved. It folds into a helix-turn-helix structure similar to those found in the tetratricopeptide repeat. Several repeats of the protein forms a ring around a single-strand RNA molecule in a sequence-sensitive way reminiscent of TAL effectors.[6]

Examples

Human genes encoding proteins containing this repeat include:

References

  1. ^ Mingler MK, Hingst AM, Clement SL, Yu LE, Reifur L, Koslowsky DJ (November 2006). "Identification of pentatricopeptide repeat proteins in Trypanosoma brucei". Mol. Biochem. Parasitol. 150 (1): 37–45. doi:10.1016/j.molbiopara.2006.06.006. PMID 16837079.
  2. ^ a b c Lurin C, Andrés C, Aubourg S, Bellaoui M, Bitton F, Bruyère C, Caboche M, Debast C, Gualberto J, Hoffmann B, Lecharny A, Le Ret M, Martin-Magniette ML, Mireau H, Peeters N, Renou JP, Szurek B, Taconnat L, Small I (August 2004). "Genome-wide analysis of Arabidopsis pentatricopeptide repeat proteins reveals their essential role in organelle biogenesis". Plant Cell. 16 (8): 2089–103. doi:10.1105/tpc.104.022236. PMC 519200. PMID 15269332.
  3. ^ O'Toole N, Hattori M, Andres C, Iida K, Lurin C, Schmitz-Linneweber C, Sugita M, Small I (June 2008). "On the expansion of the pentatricopeptide repeat gene family in plants". Mol. Biol. Evol. 25 (6): 1120–8. doi:10.1093/molbev/msn057. PMID 18343892.
  4. ^ Kotera E, Tasaka M, Shikanai T (January 2005). "A pentatricopeptide repeat protein is essential for RNA editing in chloroplasts". Nature. 433 (7023): 326–30. doi:10.1038/nature03229. PMID 15662426.
  5. ^ Takenaka M, Verbitskiy D, Zehrmann A, Brennicke A (June 2010). "Reverse genetic screening identifies five E-class PPR-proteins involved in RNA editing in mitochondria of Arabidopsis Thaliana". J Biol Chem. 285 (35): 27122–27129. doi:10.1074/jbc.M110.128611. PMC 2930711. PMID 20566637.
  6. ^ Yin P, Li Q, Yan C, Liu Y, Liu J, Yu F, et al. (December 2013). "Structural basis for the modular recognition of single-stranded RNA by PPR proteins". Nature. 504 (7478): 168–71. doi:10.1038/nature12651. PMID 24162847.


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.

PPR repeat Provide feedback

This repeat has no known function. It is about 35 amino acids long and found in up to 18 copies in some proteins. This family appears to be greatly expanded in plants. This repeat occurs in PET309 P32522 that may be involved in RNA stabilisation [1]. This domain occurs in crp1 that is involved in RNA processing [2]. This repeat is associated with a predicted plant protein O49549 that has a domain organisation similar to the human BRCA1 protein. The repeat has been called PPR [3].

Literature references

  1. Manthey GM, McEwen JE; , EMBO J 1995;14:4031-4043.: The product of the nuclear gene PET309 is required for translation of mature mRNA and stability or production of intron-containing RNAs derived from the mitochondrial COX1 locus of Saccharomyces cerevisiae. PUBMED:7664742 EPMC:7664742

  2. Barkan A, Walker M, Nolasco M, Johnson D; , EMBO J 1994;13:3170-3181.: A nuclear mutation in maize blocks the processing and translation of several chloroplast mRNAs and provides evidence for the differential translation of alternative mRNA forms. PUBMED:8039510 EPMC:8039510

  3. Small ID, Peeters I; , Trends Biochem Sci 2000;25:45-47.: The PPR motif - a TPR-related motif prevalent in plant organellar proteins. PUBMED:10664580 EPMC:10664580


Internal database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR002885

This entry represents the PPR repeat.

Pentatricopeptide repeat (PPR) proteins are characterised by tandem repeats of a degenerate 35 amino acid motif [ PUBMED:10664580 ]. PPR proteins are sequence-specific RNA-binding proteins that are involved in multiple aspects of RNA metabolism [ PUBMED:18031283 , PUBMED:22576772 ]. They can bind a diversity of sequences that confers the variability in its functions [ PUBMED:30125002 ]. Most have roles in mitochondria or plastids [ PUBMED:15270678 ]. PPR repeats were discovered while screening Arabidopsis proteins for those predicted to be targeted to mitochondria or chloroplast [ PUBMED:10664580 , PUBMED:15269332 ]. Some of these proteins have been shown to play a role in post-transcriptional processes within organelles [ PUBMED:12782738 , PUBMED:12832482 ]. Plant genomes have between one hundred to five hundred PPR genes per genome whereas non-plant genomes encode two to six PPR proteins.

The plant PPR protein family has been divided in two subfamilies on the basis of their motif content and organisation [ PUBMED:15269332 , PUBMED:17560114 ].

The crystal structure of maize chloroplast PPR10 has been reported. The nineteen repeats of PPR10 are assembled into a right-handed superhelical spiral. PPR10 forms a homodimer and exhibits considerable conformational changes upon binding to its ssRNA target, with six nucleotides being specifically recognized by six corresponding PPR10 repeats [ PUBMED:24162847 ].

Domain organisation

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

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Pfam Clan

This family is a member of clan TPR (CL0020), which has the following description:

Tetratricopeptide-like repeats are found in a numerous and diverse proteins involved in such functions as cell cycle regulation, transcriptional control, mitochondrial and peroxisomal protein transport, neurogenesis and protein folding.

The clan contains the following 176 members:

Adaptin_N Alkyl_sulf_dimr ANAPC3 ANAPC5 ANAPC8 APC_rep API5 Arm Arm_2 Arm_3 Arm_vescicular Atx10homo_assoc B56 BAF250_C BTAD CAS_CSE1 ChAPs CHIP_TPR_N CID CLASP_N Clathrin Clathrin-link Clathrin_H_link Clathrin_propel Cnd1 Cnd3 Coatomer_E Cohesin_HEAT Cohesin_load ComR_TPR COPI_C CPL CRM1_C CRM1_repeat CRM1_repeat_3 Cse1 CTK3 DHR-2 DIL DNA_alkylation Dopey_N Drf_FH3 Drf_GBD DUF1822 DUF2019 DUF2225 DUF3385 DUF3458_C DUF3808 DUF3856 DUF4042 DUF5588 DUF5691 DUF6340 DUF6377 DUF924 EAD11 EST1 EST1_DNA_bind FAT Fis1_TPR_C Fis1_TPR_N Foie-gras_1 GUN4_N HAT HEAT HEAT_2 HEAT_EZ HEAT_PBS HEAT_UF HemY_N HrpB1_HrpK HSM3_C HSM3_N IBB IBN_N IFRD Importin_rep Importin_rep_2 Importin_rep_3 Importin_rep_4 Importin_rep_5 Importin_rep_6 Insc_C KAP Leuk-A4-hydro_C LRV LRV_FeS MA3 MIF4G MIF4G_like MIF4G_like_2 MMS19_C Mo25 MRP-S27 Mtf2 NARP1 Neurochondrin Nipped-B_C Nro1 NSF Paf67 ParcG PC_rep PHAT PI3Ka PknG_TPR PPP5 PPR PPR_1 PPR_2 PPR_3 PPR_long PPTA Proteasom_PSMB PUF Rapsyn_N RIX1 RNPP_C RPM2 RPN7 Sel1 SHNi-TPR SNAP SPO22 SRP_TPR_like ST7 Suf SusD-like SusD-like_2 SusD-like_3 SusD_RagB SYCP2_ARLD TAF6_C TAL_effector TAtT Tcf25 TIP120 TOM20_plant TPR_1 TPR_10 TPR_11 TPR_12 TPR_14 TPR_15 TPR_16 TPR_17 TPR_18 TPR_19 TPR_2 TPR_20 TPR_21 TPR_22 TPR_3 TPR_4 TPR_5 TPR_6 TPR_7 TPR_8 TPR_9 TPR_MalT TTC7_N UNC45-central Upf2 V-ATPase_H_C V-ATPase_H_N Vac14_Fab1_bd Vitellogenin_N Vps39_1 W2 WSLR Wzy_C_2 Xpo1 YcaO_C YfiO Zmiz1_N

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
(458)
Full
(241615)
Representative proteomes UniProt
(375090)
RP15
(27305)
RP35
(138387)
RP55
(209383)
RP75
(271511)
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PP/heatmap 1            

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(458)
Full
(241615)
Representative proteomes UniProt
(375090)
RP15
(27305)
RP35
(138387)
RP55
(209383)
RP75
(271511)
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
(458)
Full
(241615)
Representative proteomes UniProt
(375090)
RP15
(27305)
RP35
(138387)
RP55
(209383)
RP75
(271511)
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: Pfam-B_874 (release 4.0)
Previous IDs: DUF17;
Type: Family
Sequence Ontology: SO:0100021
Author: Bateman A , Birney E
Number in seed: 458
Number in full: 241615
Average length of the domain: 29.30 aa
Average identity of full alignment: 21 %
Average coverage of the sequence by the domain: 14.69 %

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 25.0 9.3
Trusted cut-off 25.0 9.4
Noise cut-off 24.9 -1000000.0
Model length: 31
Family (HMM) version: 22
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 PPR domain has been found. There are 26 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
A0A096Q9E4 View 3D Structure Click here
A0A096Q9E4 View 3D Structure Click here
A0A096Q9E4 View 3D Structure Click here
A0A096Q9E4 View 3D Structure Click here
A0A096QEP8 View 3D Structure Click here
A0A096QEP8 View 3D Structure Click here
A0A096QEP8 View 3D Structure Click here
A0A096QZD3 View 3D Structure Click here
A0A096QZD3 View 3D Structure Click here
A0A096QZD3 View 3D Structure Click here
A0A096R0S2 View 3D Structure Click here
A0A096R0S2 View 3D Structure Click here
A0A096R0S2 View 3D Structure Click here
A0A096R0S2 View 3D Structure Click here
A0A096R0S2 View 3D Structure Click here
A0A096R0S2 View 3D Structure Click here
A0A096RDL4 View 3D Structure Click here
A0A096RDL4 View 3D Structure Click here
A0A096RDL4 View 3D Structure Click here
A0A096RDL4 View 3D Structure Click here
A0A096RDL4 View 3D Structure Click here
A0A096TBR6 View 3D Structure Click here
A0A096TBR6 View 3D Structure Click here
A0A0N7KCE8 View 3D Structure Click here
A0A0N7KCE8 View 3D Structure Click here
A0A0N7KCE8 View 3D Structure Click here
A0A0N7KCI8 View 3D Structure Click here
A0A0N7KCI8 View 3D Structure Click here
A0A0N7KCI8 View 3D Structure Click here
A0A0N7KCI8 View 3D Structure Click here
A0A0N7KDH3 View 3D Structure Click here
A0A0N7KDH3 View 3D Structure Click here
A0A0N7KDH3 View 3D Structure Click here
A0A0N7KHP0 View 3D Structure Click here
A0A0N7KPI0 View 3D Structure Click here
A0A0N7KPI0 View 3D Structure Click here
A0A0N7KPI0 View 3D Structure Click here
A0A0N7KPK3 View 3D Structure Click here
A0A0N7KPK3 View 3D Structure Click here
A0A0N7KPK3 View 3D Structure Click here
A0A0N7KSD6 View 3D Structure Click here
A0A0N7KSD6 View 3D Structure Click here
A0A0N7KTW7 View 3D Structure Click here
A0A0N7KTW7 View 3D Structure Click here
A0A0N7KTW7 View 3D Structure Click here
A0A0N7KTW7 View 3D Structure Click here
A0A0N7KTW7 View 3D Structure Click here
A0A0N7KTW7 View 3D Structure Click here
A0A0N7KTW7 View 3D Structure Click here
A0A0N7KTW7 View 3D Structure Click here
A0A0N7KTW7 View 3D Structure Click here
A0A0N7KTW7 View 3D Structure Click here
A0A0N7KTW7 View 3D Structure Click here
A0A0N7KTW7 View 3D Structure Click here
A0A0N7KTW7 View 3D Structure Click here
A0A0P0UZ80 View 3D Structure Click here
A0A0P0UZ80 View 3D Structure Click here
A0A0P0UZ80 View 3D Structure Click here
A0A0P0UZ80 View 3D Structure Click here
A0A0P0V1C9 View 3D Structure Click here
A0A0P0V1H7 View 3D Structure Click here
A0A0P0V1H7 View 3D Structure Click here
A0A0P0V1H7 View 3D Structure Click here
A0A0P0V1H7 View 3D Structure Click here
A0A0P0V1K3 View 3D Structure Click here
A0A0P0V399 View 3D Structure Click here
A0A0P0V399 View 3D Structure Click here
A0A0P0V399 View 3D Structure Click here
A0A0P0V3T7 View 3D Structure Click here
A0A0P0V3T7 View 3D Structure Click here
A0A0P0V4P7 View 3D Structure Click here
A0A0P0V4P7 View 3D Structure Click here
A0A0P0V4P7 View 3D Structure Click here
A0A0P0V4P7 View 3D Structure Click here
A0A0P0V4P7 View 3D Structure Click here
A0A0P0V4P7 View 3D Structure Click here
A0A0P0V4V8 View 3D Structure Click here
A0A0P0V4V8 View 3D Structure Click here
A0A0P0V4V8 View 3D Structure Click here
A0A0P0V4V8 View 3D Structure Click here
A0A0P0V7C6 View 3D Structure Click here
A0A0P0V7C6 View 3D Structure Click here
A0A0P0V9J9 View 3D Structure Click here
A0A0P0V9J9 View 3D Structure Click here
A0A0P0V9J9 View 3D Structure Click here
A0A0P0V9J9 View 3D Structure Click here
A0A0P0VBD6 View 3D Structure Click here
A0A0P0VBD6 View 3D Structure Click here
A0A0P0VBD6 View 3D Structure Click here
A0A0P0VBD6 View 3D Structure Click here
A0A0P0VBD6 View 3D Structure Click here
A0A0P0VC08 View 3D Structure Click here
A0A0P0VC08 View 3D Structure Click here
A0A0P0VC08 View 3D Structure Click here
A0A0P0VD44 View 3D Structure Click here
A0A0P0VD44 View 3D Structure Click here
A0A0P0VD44 View 3D Structure Click here
A0A0P0VD44 View 3D Structure Click here
A0A0P0VD44 View 3D Structure Click here
A0A0P0VDP7 View 3D Structure Click here
A0A0P0VDP7 View 3D Structure Click here
A0A0P0VDP7 View 3D Structure Click here
A0A0P0VDP7 View 3D Structure Click here
A0A0P0VDP7 View 3D Structure Click here
A0A0P0VE04 View 3D Structure Click here
A0A0P0VE04 View 3D Structure Click here
A0A0P0VE04 View 3D Structure Click here
A0A0P0VE04 View 3D Structure Click here
A0A0P0VE04 View 3D Structure Click here
A0A0P0VED0 View 3D Structure Click here
A0A0P0VED0 View 3D Structure Click here
A0A0P0VED0 View 3D Structure Click here
A0A0P0VEJ3 View 3D Structure Click here
A0A0P0VRC2 View 3D Structure Click here
A0A0P0VRC2 View 3D Structure Click here
A0A0P0VS67 View 3D Structure Click here
A0A0P0VTK8 View 3D Structure Click here
A0A0P0VTK8 View 3D Structure Click here
A0A0P0VTK8 View 3D Structure Click here
A0A0P0VTK8 View 3D Structure Click here
A0A0P0VVG0 View 3D Structure Click here
A0A0P0VVG0 View 3D Structure Click here
A0A0P0VXU3 View 3D Structure Click here
A0A0P0VYI2 View 3D Structure Click here
A0A0P0VYI2 View 3D Structure Click here
A0A0P0VZ90 View 3D Structure Click here
A0A0P0VZ90 View 3D Structure Click here
A0A0P0VZ90 View 3D Structure Click here
A0A0P0W276 View 3D Structure Click here
A0A0P0W276 View 3D Structure Click here
A0A0P0W276 View 3D Structure Click here
A0A0P0W2R9 View 3D Structure Click here
A0A0P0W2R9 View 3D Structure Click here
A0A0P0W2R9 View 3D Structure Click here
A0A0P0W2R9 View 3D Structure Click here
A0A0P0W365 View 3D Structure Click here
A0A0P0W365 View 3D Structure Click here
A0A0P0W3D2 View 3D Structure Click here
A0A0P0W3D2 View 3D Structure Click here
A0A0P0W3D2 View 3D Structure Click here
A0A0P0W3D2 View 3D Structure Click here
A0A0P0W403 View 3D Structure Click here
A0A0P0W403 View 3D Structure Click here
A0A0P0W4J2 View 3D Structure Click here
A0A0P0W4J2 View 3D Structure Click here
A0A0P0W4J2 View 3D Structure Click here
A0A0P0W4J2 View 3D Structure Click here
A0A0P0W7J8 View 3D Structure Click here
A0A0P0W7L2 View 3D Structure Click here
A0A0P0W7L2 View 3D Structure Click here
A0A0P0W8Y0 View 3D Structure Click here
A0A0P0W9E5 View 3D Structure Click here
A0A0P0W9E5 View 3D Structure Click here
A0A0P0WAE0 View 3D Structure Click here
A0A0P0WAE0 View 3D Structure Click here
A0A0P0WAE0 View 3D Structure Click here
A0A0P0WAE0 View 3D Structure Click here
A0A0P0WAE0 View 3D Structure Click here
A0A0P0WAE0 View 3D Structure Click here
A0A0P0WAE0 View 3D Structure Click here
A0A0P0WAE0 View 3D Structure Click here
A0A0P0WBL1 View 3D Structure Click here
A0A0P0WBV7 View 3D Structure Click here
A0A0P0WBV7 View 3D Structure Click here
A0A0P0WC23 View 3D Structure Click here
A0A0P0WC23 View 3D Structure Click here
A0A0P0WC23 View 3D Structure Click here
A0A0P0WEN6 View 3D Structure Click here
A0A0P0WEN6 View 3D Structure Click here
A0A0P0WEN6 View 3D Structure Click here
A0A0P0WGB0 View 3D Structure Click here
A0A0P0WGL0 View 3D Structure Click here
A0A0P0WGL0 View 3D Structure Click here
A0A0P0WKG3 View 3D Structure Click here
A0A0P0WKI2 View 3D Structure Click here
A0A0P0WKI2 View 3D Structure Click here
A0A0P0WKI2 View 3D Structure Click here
A0A0P0WKI2 View 3D Structure Click here
A0A0P0WKJ4 View 3D Structure Click here
A0A0P0WM96 View 3D Structure Click here
A0A0P0WM96 View 3D Structure Click here
A0A0P0WM96 View 3D Structure Click here
A0A0P0WMH1 View 3D Structure Click here
A0A0P0WMH1 View 3D Structure Click here
A0A0P0WMH1 View 3D Structure Click here
A0A0P0WRD6 View 3D Structure Click here
A0A0P0WRD6 View 3D Structure Click here
A0A0P0WS99 View 3D Structure Click here
A0A0P0WS99 View 3D Structure Click here
A0A0P0WTW7 View 3D Structure Click here
A0A0P0WTW7 View 3D Structure Click here
A0A0P0WTW7 View 3D Structure Click here
A0A0P0WUN7 View 3D Structure Click here
A0A0P0WUN7 View 3D Structure Click here
A0A0P0WUN7 View 3D Structure Click here
A0A0P0WUN7 View 3D Structure Click here
A0A0P0WUN7 View 3D Structure Click here
A0A0P0WUY2 View 3D Structure Click here
A0A0P0WXT3 View 3D Structure Click here
A0A0P0X070 View 3D Structure Click here
A0A0P0X098 View 3D Structure Click here
A0A0P0X098 View 3D Structure Click here
A0A0P0X098 View 3D Structure Click here
A0A0P0X098 View 3D Structure Click here
A0A0P0X0Q0 View 3D Structure Click here
A0A0P0X0Q1 View 3D Structure Click here
A0A0P0X0Q1 View 3D Structure Click here
A0A0P0X0Q1 View 3D Structure Click here
A0A0P0X2V9 View 3D Structure Click here
A0A0P0X2V9 View 3D Structure Click here
A0A0P0X2V9 View 3D Structure Click here
A0A0P0X2V9 View 3D Structure Click here
A0A0P0X3I4 View 3D Structure Click here
A0A0P0X3I4 View 3D Structure Click here
A0A0P0X3I4 View 3D Structure Click here
A0A0P0X3I4 View 3D Structure Click here
A0A0P0X4B2 View 3D Structure Click here
A0A0P0X4B2 View 3D Structure Click here
A0A0P0X4B2 View 3D Structure Click here
A0A0P0X4B2 View 3D Structure Click here
A0A0P0X5X6 View 3D Structure Click here
A0A0P0X5X6 View 3D Structure Click here
A0A0P0X6C6 View 3D Structure Click here
A0A0P0X6C6 View 3D Structure Click here
A0A0P0X8U1 View 3D Structure Click here
A0A0P0X8U1 View 3D Structure Click here
A0A0P0XBZ1 View 3D Structure Click here
A0A0P0XBZ1 View 3D Structure Click here
A0A0P0XBZ1 View 3D Structure Click here
A0A0P0XHW7 View 3D Structure Click here
A0A0P0XHW7 View 3D Structure Click here
A0A0P0XI18 View 3D Structure Click here
A0A0P0XI18 View 3D Structure Click here
A0A0P0XI18 View 3D Structure Click here
A0A0P0XNN2 View 3D Structure Click here
A0A0P0XNN2 View 3D Structure Click here
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