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35  structures 1504  species 0  interactions 193024  sequences 1384  architectures

Family: Mito_carr (PF00153)

Summary: Mitochondrial carrier protein

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 "Mitochondrial carrier". More...

Mitochondrial carrier Edit Wikipedia article

1okc opm.png
Mitochondrial ADP/ATP carrier
Identifiers
SymbolMito_carr
PfamPF00153
InterProIPR001993
PROSITEPDOC00189
SCOPe1okc / SUPFAM
TCDB2.A.29
OPM superfamily21
OPM protein1okc

Mitochondrial carriers are proteins from a solute carrier family which transfer molecules across the membranes of the mitochondria.[1] Mitochondrial carriers are also classified in the Transporter Classification Database. The Mitochondrial Carrier (MC) Superfamily has been expanded to include both the original Mitochondrial Carrier (MC) family (TC# 2.A.29) and the Mitochondrial Inner/Outer Membrane Fusion (MMF) family (TC# 9.B.25).[2]

Phylogeny

Members of the MC family (TC# 2.A.29) are found exclusively in eukaryotic organelles although they are nuclearly encoded. Most are found in mitochondria, but some are found in peroxisomes of animals, in hydrogenosomes of anaerobic fungi, and in amyloplasts of plants.

15 paralogues of the MC family are encoded within the genome of Saccharomyces cerevisiae. 50 have been identified in humans, 58 in A. thaliana and 35 in S. cerevisiae. The functions of many of the human homologues are unknown, but most of the yeast homologues have been functionally identified.[3][4] See TCDB for functional assignments

Function

Many MC proteins preferentially catalyze the exchange of one solute for another (antiport). A variety of these substrate carrier proteins, which are involved in energy transfer, have been found in the inner membranes of mitochondria and other eukaryotic organelles such as the peroxisome and facilitate the transport of inorganic ions, nucleotides, amino acids, keto acids and cofactors across the membrane.[5][6][7][8] Such proteins include:

Functional aspects of these proteins, including metabolite transport, have been reviewed by Dr. Ferdinando Palmieri and Dr. Ciro Leonardo Pierri (2010).[12][13][14] Diseases caused by defects of mitochondrial carriers are reviewed by Palmieri et al. (2008) and by Gutiérrez-Aguilar and Baines 2013.[15][16] Mutations of mitochondrial carrier genes involved in mitochondrial functions other than oxidative phosphorylation are responsible for carnitine/acylcarnitine carrier deficiency, HHH syndrome, aspartate/glutamate isoform 2 deficiency, Amish microcephaly, and neonatal myoclonic epilepsy. These disorders are characterized by specific metabolic dysfunctions, depending on the physiological role of the affected carrier in intermediary metabolism. Defects of mitochondrial carriers that supply mitochondria with the substrates of oxidative phosphorylation, inorganic phosphate and ADP, are responsible for diseases characterized by defective energy production.[15] Residues involved in substrate binding in the middle of the transporter and gating have been identified and analyzed.[8]

Structure

Permeases of the MC family (the human SLC25 family) possess six transmembrane α-helices. The proteins are of fairly uniform size of about 300 residues. They arose by tandem intragenic triplication in which a genetic element encoding two spanners gave rise to one encoding six spanners.[17] This event may have occurred less than 2 billion years ago when mitochondria first developed their specialized endosymbiotic functions within eukaryotic cells.[18] Members of the MC family are functional and structural monomers although early reports indicated that they are dimers.[3][4]

Most MC proteins contain a primary structure exhibiting three repeats, each of about 100 amino acid residues in length, and both the N and C termini face the intermembrane space. All carriers contain a common sequence, referred to as the MCF motif, in each repeated region, with some variation in one or two signature sequences.[1]

Amongst the members of the mitochondrial carrier family that have been identified, it is the ADP/ATP carrier (AAC; TC# 2.A.29.1.1) that is responsible for importing ADP into the mitochondria and exporting ATP out of the mitochondria and into the cytosol following synthesis.[19] The AAC is an integral membrane protein that is synthesised lacking a cleavable presequence, but instead contains internal targeting information.[20] It consists of a basket shaped structure with six transmembrane helices that are tilted with respect to the membrane, 3 of them "kinked" due to the presence of prolyl residues.[1]

Residues that are important for the transport mechanism are likely to be symmetrical, whereas residues involved in substrate binding will be asymmetrical reflecting the asymmetry of the substrates. By scoring the symmetry of residues in the sequence repeats, Robinson et al. (2008) identified the substrate-binding sites and salt bridge networks that are important for transport. The symmetry analyses provides an assessment of the role of residues and provides clues to the chemical identities of substrates of uncharacterized transporters.[21]

There are structures of the mitochondrial ADP/ATP carrier in two different states. One is the cytoplasmic state, inhibited by carboxyatractyloside, in which the substrate binding site is accessible to the intermembrane space, which is confluent with the cytosol, i.e. the bovine mitochondrial ADP/ATP carrier PDB: 1OKC​/PDB: 2C3E​,[22][23] the yeast ADP/ATP carrier Aac2p PDB: 4C9G​/PDB: 4C9H​,[24] the yeast ADP/ATP carrier Aac3p PDB: 4C9J​/PDB: 4C9Q​,[24] Another is the matrix state, inhibited by bongkrekic acid, in which the substrate binding site is accessible to the mitochondrial matrix, i.e. the fungal mitochondrial ADP/ATP carrier PDB: 6GCI​.[25] In addition, there are structures of the calcium regulatory domains of the mitochondrial ATP-Mg/Pi carrier in the calcium-bound state PDB: 4ZCU​/PDB: 4N5X[26][27] and mitochondrial aspartate/glutamate carriers in different regulatory states PDB: 4P5X​/PDB: 4P60​/PDB: 4P5W​.[28]

Substrates

Mitochondrial carriers transport amino acids, keto acids, nucleotides, inorganic ions and co-factors through the mitochondrial inner membrane. The transporters consist of six transmembrane alpha-helices with threefold pseudo-symmetry.[29]

The transported substrates of MC family members may bind to the bottom of the cavity, and translocation results in a transient transition from a 'pit' to a 'channel' conformation.[30] An inhibitor of AAC, carboxyatractyloside, probably binds where ADP binds, in the pit on the outer surface, thus blocking the transport cycle. Another inhibitor, bongkrekic acid, is believed to stabilize a second conformation, with the pit facing the matrix. In this conformation, the inhibitor may bind to the ATP-binding site. Functional and structural roles for residues in the TMSs have been proposed.[31][32] The mitochondrial carrier signature, Px[D/E]xx[K/R], of carriers is probably involved both in the biogenesis and in the transport activity of these proteins.[33] A homologue has been identified in the mimivirus genome and shown to be a transporter for dATP and dTTP.[34]

Examples of transported compounds include:

Examples

Human proteins containing this domain include:

References

  1. ^ a b c Nury, H.; Dahout-Gonzalez, C.; Trézéguet, V.; Lauquin, G.J.M.; Brandolin, G.; Pebay-Peyroula, E. (2006). "Relations between structure and function of the mitochondrial ADP/ATP carrier". Annu. Rev. Biochem. 75: 713–41. doi:10.1146/annurev.biochem.75.103004.142747. PMID 16756509.
  2. ^ Kuan J, Saier MH (October 1993). "Expansion of the mitochondrial carrier family". Research in Microbiology. 144 (8): 671–2. doi:10.1016/0923-2508(93)90073-B. PMID 8140286.
  3. ^ a b Bamber L, Harding M, Monné M, Slotboom DJ, Kunji ER (June 2007). "The yeast mitochondrial ADP/ATP carrier functions as a monomer in mitochondrial membranes". Proceedings of the National Academy of Sciences of the United States of America. 104 (26): 10830–4. Bibcode:2007PNAS..10410830B. doi:10.1073/pnas.0703969104. PMC 1891095. PMID 17566106.
  4. ^ a b Bamber L, Harding M, Butler PJ, Kunji ER (October 2006). "Yeast mitochondrial ADP/ATP carriers are monomeric in detergents". Proceedings of the National Academy of Sciences of the United States of America. 103 (44): 16224–9. Bibcode:2006PNAS..10316224B. doi:10.1073/pnas.0607640103. PMC 1618811. PMID 17056710.
  5. ^ Klingenberg M (March 1990). "Mechanism and evolution of the uncoupling protein of brown adipose tissue". Trends in Biochemical Sciences. 15 (3): 108–12. doi:10.1016/0968-0004(90)90194-G. PMID 2158156.
  6. ^ Nelson DR, Lawson JE, Klingenberg M, Douglas MG (April 1993). "Site-directed mutagenesis of the yeast mitochondrial ADP/ATP translocator. Six arginines and one lysine are essential". Journal of Molecular Biology. 230 (4): 1159–70. doi:10.1006/jmbi.1993.1233. PMID 8487299.
  7. ^ Jank B, Habermann B, Schweyen RJ, Link TA (November 1993). "PMP47, a peroxisomal homologue of mitochondrial solute carrier proteins". Trends in Biochemical Sciences. 18 (11): 427–8. doi:10.1016/0968-0004(93)90141-9. PMID 8291088.
  8. ^ a b Monné M, Palmieri F, Kunji ER (March 2013). "The substrate specificity of mitochondrial carriers: mutagenesis revisited". Molecular Membrane Biology. 30 (2): 149–59. doi:10.3109/09687688.2012.737936. PMID 23121155.
  9. ^ a b Dolce V, Cappello AR, Capobianco L (July 2014). "Mitochondrial tricarboxylate and dicarboxylate-tricarboxylate carriers: from animals to plants". IUBMB Life. 66 (7): 462–71. doi:10.1002/iub.1290. PMID 25045044.
  10. ^ Palmieri F (June 1994). "Mitochondrial carrier proteins". FEBS Letters. 346 (1): 48–54. doi:10.1016/0014-5793(94)00329-7. PMID 8206158.
  11. ^ Walker JE (1992). "The mitochondrial transporter family". Curr. Opin. Struct. Biol. 2 (4): 519–526. doi:10.1016/0959-440X(92)90081-H.
  12. ^ Palmieri F (February 2004). "The mitochondrial transporter family (SLC25): physiological and pathological implications". Pflügers Archiv. 447 (5): 689–709. doi:10.1007/s00424-003-1099-7. PMID 14598172.
  13. ^ Palmieri F, Rieder B, Ventrella A, Blanco E, Do PT, Nunes-Nesi A, Trauth AU, Fiermonte G, Tjaden J, Agrimi G, Kirchberger S, Paradies E, Fernie AR, Neuhaus HE (November 2009). "Molecular identification and functional characterization of Arabidopsis thaliana mitochondrial and chloroplastic NAD+ carrier proteins". The Journal of Biological Chemistry. 284 (45): 31249–59. doi:10.1074/jbc.M109.041830. PMC 2781523. PMID 19745225.
  14. ^ Palmieri F, Pierri CL (2010-01-01). "Mitochondrial metabolite transport". Essays in Biochemistry. 47: 37–52. doi:10.1042/bse0470037. PMID 20533899.
  15. ^ a b Palmieri F (2008-08-01). "Diseases caused by defects of mitochondrial carriers: a review". Biochimica et Biophysica Acta. 1777 (7–8): 564–78. doi:10.1016/j.bbabio.2008.03.008. PMID 18406340.
  16. ^ Gutiérrez-Aguilar M, Baines CP (September 2013). "Physiological and pathological roles of mitochondrial SLC25 carriers". The Biochemical Journal. 454 (3): 371–86. doi:10.1042/BJ20121753. PMC 3806213. PMID 23988125.
  17. ^ Palmieri F (2013-06-01). "The mitochondrial transporter family SLC25: identification, properties and physiopathology". Molecular Aspects of Medicine. 34 (2–3): 465–84. doi:10.1016/j.mam.2012.05.005. PMID 23266187.
  18. ^ Kuan J, Saier MH (1993-01-01). "The mitochondrial carrier family of transport proteins: structural, functional, and evolutionary relationships". Critical Reviews in Biochemistry and Molecular Biology. 28 (3): 209–33. doi:10.3109/10409239309086795. PMID 8325039.
  19. ^ Kunji, Edmund R. S.; Aleksandrova, Antoniya; King, Martin S.; Majd, Homa; Ashton, Valerie L.; Cerson, Elizabeth; Springett, Roger; Kibalchenko, Mikhail; Tavoulari, Sotiria (2016). "The transport mechanism of the mitochondrial ADP/ATP carrier" (PDF). Biochimica et Biophysica Acta. 1863 (10): 2379–2393. doi:10.1016/j.bbamcr.2016.03.015. ISSN 0006-3002. PMID 27001633.
  20. ^ Ryan MT, Müller H, Pfanner N (July 1999). "Functional staging of ADP/ATP carrier translocation across the outer mitochondrial membrane". The Journal of Biological Chemistry. 274 (29): 20619–27. doi:10.1074/jbc.274.29.20619. PMID 10400693.
  21. ^ Robinson AJ, Overy C, Kunji ER (November 2008). "The mechanism of transport by mitochondrial carriers based on analysis of symmetry". Proceedings of the National Academy of Sciences of the United States of America. 105 (46): 17766–71. Bibcode:2008PNAS..10517766R. doi:10.1073/pnas.0809580105. PMC 2582046. PMID 19001266.
  22. ^ Pebay-Peyroula, Eva; Dahout-Gonzalez, Cécile; Kahn, Richard; Trézéguet, Véronique; Lauquin, Guy J.-M.; Brandolin, Gérard (2003). "Structure of mitochondrial ADP/ATP carrier in complex with carboxyatractyloside". Nature. 426 (6962): 39–44. Bibcode:2003Natur.426...39P. doi:10.1038/nature02056. ISSN 1476-4687. PMID 14603310.
  23. ^ Nury, H.; Dahout-Gonzalez, C.; Trézéguet, V.; Lauquin, G.; Brandolin, G.; Pebay-Peyroula, E. (2005). "Structural basis for lipid-mediated interactions between mitochondrial ADP/ATP carrier monomers". FEBS Letters. 579 (27): 6031–6036. doi:10.1016/j.febslet.2005.09.061. ISSN 0014-5793. PMID 16226253.
  24. ^ a b Ruprecht, Jonathan J.; Hellawell, Alex M.; Harding, Marilyn; Crichton, Paul G.; McCoy, Airlie J.; Kunji, Edmund R. S. (2014). "Structures of yeast mitochondrial ADP/ATP carriers support a domain-based alternating-access transport mechanism". Proceedings of the National Academy of Sciences of the United States of America. 111 (4): E426–434. Bibcode:2014PNAS..111E.426R. doi:10.1073/pnas.1320692111. ISSN 1091-6490. PMC 3910652. PMID 24474793.
  25. ^ Ruprecht, Jonathan J.; King, Martin S.; Zögg, Thomas; Aleksandrova, Antoniya A.; Pardon, Els; Crichton, Paul G.; Steyaert, Jan; Kunji, Edmund R. S. (2019). "The Molecular Mechanism of Transport by the Mitochondrial ADP/ATP Carrier". Cell. 176 (3): 435–447.e15. doi:10.1016/j.cell.2018.11.025. ISSN 1097-4172. PMC 6349463. PMID 30611538.
  26. ^ Harborne, Steven P. D.; Ruprecht, Jonathan J.; Kunji, Edmund R. S. (2015). "Calcium-induced conformational changes in the regulatory domain of the human mitochondrial ATP-Mg/Pi carrier". Biochimica et Biophysica Acta. 1847 (10): 1245–1253. doi:10.1016/j.bbabio.2015.07.002. ISSN 0006-3002. PMC 4562336. PMID 26164100.
  27. ^ Yang, Qin; Brüschweiler, Sven; Chou, James J. (2014). "A self-sequestered calmodulin-like Ca²⁺ sensor of mitochondrial SCaMC carrier and its implication to Ca²⁺-dependent ATP-Mg/P(i) transport". Structure. 22 (2): 209–217. doi:10.1016/j.str.2013.10.018. ISSN 1878-4186. PMC 3946054. PMID 24332718.
  28. ^ Thangaratnarajah, Chancievan; Ruprecht, Jonathan J.; Kunji, Edmund R. S. (2014). "Calcium-induced conformational changes of the regulatory domain of human mitochondrial aspartate/glutamate carriers". Nature Communications. 5: 5491. Bibcode:2014NatCo...5.5491T. doi:10.1038/ncomms6491. ISSN 2041-1723. PMC 4250520. PMID 25410934.
  29. ^ Kunji ER, Robinson AJ (August 2010). "Coupling of proton and substrate translocation in the transport cycle of mitochondrial carriers". Current Opinion in Structural Biology. 20 (4): 440–7. doi:10.1016/j.sbi.2010.06.004. PMID 20598524.
  30. ^ Kunji ER, Robinson AJ (2006-10-01). "The conserved substrate binding site of mitochondrial carriers". Biochimica et Biophysica Acta. 1757 (9–10): 1237–48. doi:10.1016/j.bbabio.2006.03.021. PMID 16759636.
  31. ^ Cappello AR, Curcio R, Valeria Miniero D, Stipani I, Robinson AJ, Kunji ER, Palmieri F (October 2006). "Functional and structural role of amino acid residues in the even-numbered transmembrane alpha-helices of the bovine mitochondrial oxoglutarate carrier". Journal of Molecular Biology. 363 (1): 51–62. doi:10.1016/j.jmb.2006.08.041. PMID 16962611.
  32. ^ Cappello AR, Miniero DV, Curcio R, Ludovico A, Daddabbo L, Stipani I, Robinson AJ, Kunji ER, Palmieri F (June 2007). "Functional and structural role of amino acid residues in the odd-numbered transmembrane alpha-helices of the bovine mitochondrial oxoglutarate carrier". Journal of Molecular Biology. 369 (2): 400–12. doi:10.1016/j.jmb.2007.03.048. PMID 17442340.
  33. ^ Zara V, Ferramosca A, Capobianco L, Baltz KM, Randel O, Rassow J, Palmieri F, Papatheodorou P (December 2007). "Biogenesis of yeast dicarboxylate carrier: the carrier signature facilitates translocation across the mitochondrial outer membrane". Journal of Cell Science. 120 (Pt 23): 4099–106. doi:10.1242/jcs.018929. PMID 18032784.
  34. ^ Monné M, Robinson AJ, Boes C, Harbour ME, Fearnley IM, Kunji ER (April 2007). "The mimivirus genome encodes a mitochondrial carrier that transports dATP and dTTP". Journal of Virology. 81 (7): 3181–6. doi:10.1128/JVI.02386-06. PMC 1866048. PMID 17229695.

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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.

Mitochondrial carrier protein Provide feedback

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Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR018108

A variety of substrate carrier proteins that are involved in energy transfer are found in the inner mitochondrial membrane or integral to the membrane of other eukaryotic organelles such as the peroxisome [ PUBMED:2158156 , PUBMED:8140286 , PUBMED:8487299 , PUBMED:8206158 , PUBMED:8291088 ]. Such proteins include: ADP, ATP carrier protein (ADP/ATP translocase); 2-oxoglutarate/malate carrier protein; phosphate carrier protein; tricarboxylate transport protein (or citrate transport protein); Graves disease carrier protein; yeast mitochondrial proteins MRS3 and MRS4; yeast mitochondrial FAD carrier protein; and many others. Structurally, these proteins can consist of up to three tandem repeats of a domain of approximately 100 residues, each domain containing two transmembrane regions.

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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(35096)
RP35
(88158)
RP55
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Full
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RP15
(35096)
RP35
(88158)
RP55
(151872)
RP75
(205761)
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  Seed
(160)
Full
(193024)
Representative proteomes UniProt
(345254)
RP15
(35096)
RP35
(88158)
RP55
(151872)
RP75
(205761)
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Trees

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Curation and family details

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Curation View help on the curation process

Seed source: Prosite
Previous IDs: mito_carr;
Type: Repeat
Sequence Ontology: SO:0001068
Author: Sonnhammer ELL
Number in seed: 160
Number in full: 193024
Average length of the domain: 94.20 aa
Average identity of full alignment: 21 %
Average coverage of the sequence by the domain: 71.39 %

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 22.3 22.3
Trusted cut-off 22.3 22.3
Noise cut-off 22.2 22.2
Model length: 97
Family (HMM) version: 29
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 Mito_carr domain has been found. There are 35 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
A0A0G2JV03 View 3D Structure Click here
A0A0G2K309 View 3D Structure Click here
A0A0G2K309 View 3D Structure Click here
A0A0G2K309 View 3D Structure Click here
A0A0G2K459 View 3D Structure Click here
A0A0G2K5L2 View 3D Structure Click here
A0A0G2K5L2 View 3D Structure Click here
A0A0G2K5L2 View 3D Structure Click here
A0A0G2KLU8 View 3D Structure Click here
A0A0G2KLU8 View 3D Structure Click here
A0A0G2KLU8 View 3D Structure Click here
A0A0G2L4H5 View 3D Structure Click here
A0A0G2L4H5 View 3D Structure Click here
A0A0G2L4H5 View 3D Structure Click here
A0A0P0UZT6 View 3D Structure Click here
A0A0P0V3K9 View 3D Structure Click here
A0A0P0VG45 View 3D Structure Click here
A0A0P0VG45 View 3D Structure Click here
A0A0P0VG45 View 3D Structure Click here
A0A0P0VGN9 View 3D Structure Click here
A0A0P0VGN9 View 3D Structure Click here
A0A0P0VGN9 View 3D Structure Click here
A0A0P0VGN9 View 3D Structure Click here
A0A0P0VTR5 View 3D Structure Click here
A0A0P0WYD6 View 3D Structure Click here
A0A0P0WYD6 View 3D Structure Click here
A0A0P0WYD6 View 3D Structure Click here
A0A0P0X501 View 3D Structure Click here
A0A0P0XP23 View 3D Structure Click here
A0A0P0XP23 View 3D Structure Click here
A0A0P0XP23 View 3D Structure Click here
A0A0P0Y1K6 View 3D Structure Click here
A0A0P0YBJ7 View 3D Structure Click here
A0A0P0YBJ7 View 3D Structure Click here
A0A0R0EB47 View 3D Structure Click here
A0A0R0EB47 View 3D Structure Click here
A0A0R0EB47 View 3D Structure Click here
A0A0R0F1Z4 View 3D Structure Click here
A0A0R0F1Z4 View 3D Structure Click here
A0A0R0F1Z4 View 3D Structure Click here
A0A0R0FLJ8 View 3D Structure Click here
A0A0R0FLJ8 View 3D Structure Click here
A0A0R0FUL1 View 3D Structure Click here
A0A0R0FUL1 View 3D Structure Click here
A0A0R0GC05 View 3D Structure Click here
A0A0R0GC05 View 3D Structure Click here
A0A0R0GET2 View 3D Structure Click here
A0A0R0GET2 View 3D Structure Click here
A0A0R0GET2 View 3D Structure Click here
A0A0R0GIS2 View 3D Structure Click here
A0A0R0GIS2 View 3D Structure Click here
A0A0R0GPW5 View 3D Structure Click here
A0A0R0GPW5 View 3D Structure Click here
A0A0R0GXN6 View 3D Structure Click here
A0A0R0GXN6 View 3D Structure Click here
A0A0R0GXN6 View 3D Structure Click here
A0A0R0H3N5 View 3D Structure Click here
A0A0R0H3N5 View 3D Structure Click here
A0A0R0HAS1 View 3D Structure Click here
A0A0R0HAS1 View 3D Structure Click here
A0A0R0HAS1 View 3D Structure Click here
A0A0R0IWF6 View 3D Structure Click here
A0A0R0IWF6 View 3D Structure Click here
A0A0R0IWF6 View 3D Structure Click here
A0A0R0IXS8 View 3D Structure Click here
A0A0R0J393 View 3D Structure Click here
A0A0R0J393 View 3D Structure Click here
A0A0R0KCZ9 View 3D Structure Click here
A0A0R0KF80 View 3D Structure Click here
A0A0R0KF80 View 3D Structure Click here
A0A0R0KF80 View 3D Structure Click here
A0A0R0KTL1 View 3D Structure Click here
A0A0R0KTL1 View 3D Structure Click here
A0A0R0KZR8 View 3D Structure Click here
A0A0R0KZR8 View 3D Structure Click here
A0A0R0L428 View 3D Structure Click here
A0A0R0L428 View 3D Structure Click here
A0A0R0L428 View 3D Structure Click here
A0A0R0L6R1 View 3D Structure Click here
A0A0R0L6R1 View 3D Structure Click here
A0A0R0L6R1 View 3D Structure Click here
A0A0R0LFF0 View 3D Structure Click here
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