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2CB8

High resolution crystal structure of liganded human L-ACBP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000062molecular_functionfatty-acyl-CoA binding
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
B0000062molecular_functionfatty-acyl-CoA binding
B0005783cellular_componentendoplasmic reticulum
B0005788cellular_componentendoplasmic reticulum lumen
B0005794cellular_componentGolgi apparatus
B0006631biological_processfatty acid metabolic process
B0008289molecular_functionlipid binding
B0030156molecular_functionbenzodiazepine receptor binding
B0032994cellular_componentprotein-lipid complex
B0036042molecular_functionlong-chain fatty acyl-CoA binding
B0036151biological_processphosphatidylcholine acyl-chain remodeling
B0042802molecular_functionidentical protein binding
B0070062cellular_componentextracellular exosome
B1903060biological_processnegative regulation of protein lipidation
B1905920biological_processpositive regulation of CoA-transferase activity
B2001140biological_processpositive regulation of phospholipid transport
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A1089
ChainResidue
AHIS31
AHOH2150
AHOH2151
BGLU7

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A1090
ChainResidue
AMYA1088
AZN1093
AMYA1094
ASO41095

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A1091
ChainResidue
AHIS15
AASP22
AMYA1094
AGLU11

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A1092
ChainResidue
ASER2
AGLU68
AHOH2152
BASP69

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A1093
ChainResidue
AMYA1088
AZN1090
AMYA1094
ASO41095

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A1095
ChainResidue
AMYA1088
AZN1090
AZN1093
AMYA1094
AZN1096

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ZN A1096
ChainResidue
AMYA1094
ASO41095

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B1090
ChainResidue
AGLU23
BGLU11
BHIS15
BHOH2131
BHOH2132

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B1091
ChainResidue
AGLU7
BMYA1088
BHOH2133
BHOH2134

site_idBC1
Number of Residues23
DetailsBINDING SITE FOR RESIDUE MYA A1088
ChainResidue
AALA10
AARG14
AILE28
ATYR29
ATYR32
ALYS33
ALYS55
ATYR74
AZN1090
AZN1093
AMYA1094
ASO41095
AHOH2026
AHOH2100
AHOH2106
AHOH2143
AHOH2144
AHOH2145
AHOH2146
AHOH2147
AHOH2148
AHOH2149
BMYA1088

site_idBC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE MYA A1094
ChainResidue
AGLU11
AARG14
AHIS15
ALYS19
AASP22
ATHR51
AMYA1088
AZN1090
AZN1091
AZN1093
ASO41095
AZN1096
AHOH2025
AHOH2106
AHOH2153
AHOH2154
AHOH2155
BMYA1088

site_idBC3
Number of Residues35
DetailsBINDING SITE FOR RESIDUE MYA B1088
ChainResidue
BMYA1089
BZN1091
BHOH2088
BHOH2123
BHOH2124
BHOH2125
BHOH2126
BHOH2127
BHOH2128
BHOH2129
BHOH2130
BHOH2133
BHOH2134
AALA4
AGLU7
ALYS8
AGLU11
AARG14
ALYS19
AASP22
AARG44
ALYS53
AALA54
AASP57
AMYA1088
AMYA1094
AHOH2114
BALA10
BARG14
BILE28
BTYR29
BTYR32
BLYS33
BLYS55
BTYR74

site_idBC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MYA B1089
ChainResidue
BVAL13
BARG14
BLEU16
BLYS19
BPRO20
BMET25
BMYA1088
BMXE1092

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MXE B1092
ChainResidue
AASP39
ATHR65
AHOH2077
BMYA1089
BHOH2045

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 Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:17044054, ECO:0007744|PDB:2CB8
ChainResidueDetails
AHIS15
AGLY30
ATRP56
AILE75
BHIS15
BGLY30
BTRP56
BILE75

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N-acetylserine => ECO:0000269|PubMed:3525533, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22814378
ChainResidueDetails
AGLN3
BGLN3

site_idSWS_FT_FI3
Number of Residues6
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P31786
ChainResidueDetails
AALA9
ATRP56
AVAL78
BALA9
BTRP56
BVAL78

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P31786
ChainResidueDetails
ATHR18
BTHR18

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
APRO20
BPRO20

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:20068231
ChainResidueDetails
AGLY30
BGLY30

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PDB entries from 2024-10-09

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