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4AYT

STRUCTURE OF THE HUMAN MITOCHONDRIAL ABC TRANSPORTER, ABCB10

Replaces:  2YL4
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 Residues4
DetailsBINDING SITE FOR RESIDUE MG A 801
ChainResidue
ASER534
AGLN575
AASP658
AACP900

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE ACP A 900
ChainResidue
AGLY530
ASER531
AGLY532
ALYS533
ASER534
ATHR535
ATYR544
AGLN575
AMG801
AHOH2055
AASP264
ATYR501
AALA503
AILE509
ASER529

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GLY A 1717
ChainResidue
AARG170
ATYR234
AARG242

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE LMT A 1720
ChainResidue
AASP197
ATYR200
ATHR201
APRO203
ALEU214
AGLY418
AMET421
ATHR427
AVAL428
AASN484
ALYS486
AHOH2033

site_idAC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE CDL A 1721
ChainResidue
APRO312
AASN313
AASN313
ATHR316
ATHR316
APHE317
APHE317
ASER405
ASER405
ALYS416
ALYS416
ALMT1724
ALMT1724

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE LMT A 1723
ChainResidue
ASER449

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE LMT A 1724
ChainResidue
ASER405
ASER412
ATYR415
ALYS416
ALEU420
ASER423
AHIS425
ACDL1721
ACDL1721
AHOH2032

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CDL A 1727
ChainResidue
APHE191
ALEU214
APHE222
AASN407

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

site_idSWS_FT_FI2
Number of Residues382
DetailsTOPO_DOM: Mitochondrial matrix => ECO:0000255
ChainResidueDetails
ALEU192-CYS215
AARG334-ASN407
ATYR452-ALA738

site_idSWS_FT_FI3
Number of Residues76
DetailsTOPO_DOM: Mitochondrial intermembrane => ECO:0000255
ChainResidueDetails
AGLN237-PRO312
AGLY429-GLU430

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

227933

PDB entries from 2024-11-27

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