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4ZV3

Crystal structure of the N- and C-terminal domains of mouse acyl-CoA thioesterase 7

Functional Information from GO Data
ChainGOidnamespacecontents
A0016790molecular_functionthiolester hydrolase activity
B0016790molecular_functionthiolester hydrolase activity
C0016790molecular_functionthiolester hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues21
Detailsbinding site for residue COA A 401
ChainResidue
AALA107
ALEU169
ATYR198
AGLN201
ALYS202
AARG205
AVAL249
AHIS250
ATHR254
AASN283
APHE284
ALEU108
AHIS285
ALYS287
AALA109
AARG110
ASER136
ALYS137
AHIS138
ASER139
AVAL167

site_idAC2
Number of Residues19
Detailsbinding site for residue COA B 401
ChainResidue
BALA107
BLEU108
BALA109
BARG110
BSER136
BLYS137
BHIS138
BSER139
BTRP165
BLEU169
BTYR198
BLYS202
BARG205
BTHR254
BASN283
BPHE284
BHIS285
BASP286
BLYS287

site_idAC3
Number of Residues18
Detailsbinding site for residue COA C 401
ChainResidue
CLEU108
CALA109
CARG110
CSER136
CLYS137
CHIS138
CSER139
CLEU169
CTYR198
CGLN201
CLYS202
CARG205
CTHR254
CASN283
CPHE284
CHIS285
CASP286
CLYS287

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:17563367
ChainResidueDetails
AASN70
AASP259
BASN70
BASP259
CASN70
CASP259

site_idSWS_FT_FI2
Number of Residues9
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:O00154
ChainResidueDetails
ALYS172
ALYS202
ALYS287
BLYS172
BLYS202
BLYS287
CLYS172
CLYS202
CLYS287

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PDB entries from 2025-06-11

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