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5ZXD

Crystal structure of ATP-bound human ABCF1

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0016887molecular_functionATP hydrolysis activity
B0005524molecular_functionATP binding
B0016887molecular_functionATP hydrolysis activity
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue ATP A 601
ChainResidue
AHIS16
AGLU179
AHOH710
AHOH759
AASN40
AGLY41
ALYS42
AGLY43
ALYS44
ATHR45
ATHR46
AASP178

site_idAC2
Number of Residues18
Detailsbinding site for residue ATP A 602
ChainResidue
ATYR336
AGLN339
ALEU342
AASN362
AGLY363
AGLY365
ALYS366
ASER367
ATHR368
AASP469
AGLU470
AHOH705
AHOH707
AHOH718
AHOH775
AHOH813
BPRO60
BASN61

site_idAC3
Number of Residues14
Detailsbinding site for residue ATP B 601
ChainResidue
BHIS16
BLYS18
BASN40
BGLY41
BLYS42
BGLY43
BLYS44
BTHR45
BTHR46
BASP178
BGLU179
BHOH701
BHOH702
BHOH714

site_idAC4
Number of Residues12
Detailsbinding site for residue ATP B 602
ChainResidue
BTYR336
BGLN339
BGLY363
BVAL364
BGLY365
BLYS366
BSER367
BTHR368
BASP469
BGLU470
BHOH709
BHOH721

Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. FSGGWRMRVSLARAL
ChainResidueDetails
APHE154-LEU168
ALEU445-ALA459

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues28
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17525332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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