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4AYW

STRUCTURE OF THE HUMAN MITOCHONDRIAL ABC TRANSPORTER, ABCB10 (PLATE FORM)

Replaces:  4AA3
Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0016020cellular_componentmembrane
A0016887molecular_functionATP hydrolysis activity
A0055085biological_processtransmembrane transport
A0140359molecular_functionABC-type transporter activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ANP A 1719
ChainResidue
AASP264
ATYR501
ASER529
AGLY530
AGLY532
ALYS533
ASER534
ATHR535

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE LMT A 1724
ChainResidue
ALEU419
AASP677
AARG678
AASP681
ALYS416

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE Y01 A 1730
ChainResidue
AARG170
AARG213
AALA227
AALA230
ATYR234
ALEU235
AARG389
APHE393
AGLY397
ALEU404

Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. LSGGQKQRIAIARAL
ChainResidueDetails
ALEU634-LEU648

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues140
DetailsTOPO_DOM: Mitochondrial intermembrane => ECO:0000255
ChainResidueDetails
AALA226-LEU290
AGLN237-PRO312
AGLY429-GLU430

site_idSWS_FT_FI2
Number of Residues100
DetailsTRANSMEM: Helical => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
ALEU171-PHE191
ALEU216-MET236
AASN313-GLY333
ALEU408-VAL428
ALEU431-PHE451

site_idSWS_FT_FI3
Number of Residues382
DetailsTOPO_DOM: Mitochondrial matrix => ECO:0000255
ChainResidueDetails
ALEU192-CYS215
AARG334-ASN407
ATYR452-ALA738

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING:
ChainResidueDetails
AGLY527

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS265

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: S-glutathionyl cysteine => ECO:0000250|UniProtKB:Q9JI39
ChainResidueDetails
ACYS582

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PDB entries from 2024-11-06

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