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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 Residues130
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"23716676","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4AYT","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues35
DetailsTopological domain: {"description":"Mitochondrial intermembrane","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues108
DetailsTopological domain: {"description":"Mitochondrial matrix","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues286
DetailsDomain: {"description":"ABC transmembrane type-1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"37041204","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7Y48","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"23716676","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4AYT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4AYX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"23716676","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4AYT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4AYW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4AYX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"23716676","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4AYT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4AYW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"23716676","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4AYT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4AYX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"S-glutathionyl cysteine","evidences":[{"source":"UniProtKB","id":"Q9JI39","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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