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2FJ9

High resolution crystal structure of the unliganded human ACBP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000062molecular_functionfatty-acyl-CoA binding
A0005739cellular_componentmitochondrion
A0005783cellular_componentendoplasmic reticulum
A0005788cellular_componentendoplasmic reticulum lumen
A0005794cellular_componentGolgi apparatus
A0006631biological_processfatty acid metabolic process
A0008289molecular_functionlipid binding
A0030156molecular_functionbenzodiazepine receptor binding
A0032994cellular_componentprotein-lipid complex
A0036042molecular_functionlong-chain fatty acyl-CoA binding
A0036151biological_processphosphatidylcholine acyl-chain remodeling
A0042802molecular_functionidentical protein binding
A0070062cellular_componentextracellular exosome
A1903060biological_processnegative regulation of protein lipidation
A1905920biological_processpositive regulation of CoA-transferase activity
A2001140biological_processpositive regulation of phospholipid transport
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PB A 1
ChainResidue
AGLU61
AASP69
ACL89
AHOH1101
AHOH1156

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 88
ChainResidue
AHOH1277
AHOH1277
AGLU11
AGLU11
AHIS15
AHIS15

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 89
ChainResidue
APB1
AGLU61
AASP69
AHOH1034

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 90
ChainResidue
AASP22
AGLU43

Functional Information from PROSITE/UniProt
site_idPS00880
Number of Residues19
DetailsACB_1 Acyl-CoA-binding (ACB) domain signature. PSdEeMlfIYGhYKQATvG
ChainResidueDetails
APRO20-GLY38

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:17044054, ECO:0007744|PDB:2CB8
ChainResidueDetails
AHIS15
AILE75
AGLY30
ATRP56

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylserine => ECO:0000269|PubMed:3525533, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22814378
ChainResidueDetails
AGLN3

site_idSWS_FT_FI3
Number of Residues3
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P31786
ChainResidueDetails
AALA9
ATRP56
AVAL78

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P31786
ChainResidueDetails
ATHR18

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
APRO20

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:20068231
ChainResidueDetails
AGLY30

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PDB entries from 2024-04-17

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