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1HB8

Structure of bovine Acyl-CoA binding protein in tetragonal crystal form

Functional Information from GO Data
ChainGOidnamespacecontents
A0000062molecular_functionfatty-acyl-CoA binding
A0005783cellular_componentendoplasmic reticulum
A0005794cellular_componentGolgi apparatus
A0006631biological_processfatty acid metabolic process
A0008289molecular_functionlipid binding
B0000062molecular_functionfatty-acyl-CoA binding
B0005783cellular_componentendoplasmic reticulum
B0005794cellular_componentGolgi apparatus
B0006631biological_processfatty acid metabolic process
B0008289molecular_functionlipid binding
C0000062molecular_functionfatty-acyl-CoA binding
C0005783cellular_componentendoplasmic reticulum
C0005794cellular_componentGolgi apparatus
C0006631biological_processfatty acid metabolic process
C0008289molecular_functionlipid binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 87
ChainResidue
ALYS50
ALYS54
BARG43
BPHE49
BLYS52

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 B 87
ChainResidue
BHOH2078
BHOH2079
CARG43
CPHE49
CLYS52
BLYS50
BLYS54
BHOH2076
BHOH2077

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 C 87
ChainResidue
AARG43
APHE49
ALYS52
BHOH2015
CLYS50
CLYS54
CHOH2080
CHOH2081
CHOH2082

Functional Information from PROSITE/UniProt
site_idPS00880
Number of Residues19
DetailsACB_1 Acyl-CoA-binding (ACB) domain signature. PAdEeMlfIYShYKQATvG
ChainResidueDetails
APRO19-GLY37

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues255
DetailsDomain: {"description":"ACB","evidences":[{"source":"PROSITE-ProRule","id":"PRU00573","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"8503960","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2003","submissionDatabase":"PDB data bank","title":"RDC-refined NMR structure of bovine acyl-coenzyme A binding protein, ACBP, in complex with palmitoyl-coenzyme A.","authors":["Lerche M.H.","Kragelund B.B.","Redfield C.","Poulsen F.M."]}},{"source":"PDB","id":"1ACA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NVL","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsModified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"3525533","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues9
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P31786","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues3
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P31786","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues3
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P07108","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues3
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P07108","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues3
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P31786","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

243083

PDB entries from 2025-10-15

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