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7DBL

Acyl-CoA hydrolase MpaH' mutant S139A in complex with MPA

Functional Information from GO Data
ChainGOidnamespacecontents
A0005782cellular_componentperoxisomal matrix
A0016114biological_processterpenoid biosynthetic process
A0016787molecular_functionhydrolase activity
A0017000biological_processantibiotic biosynthetic process
A0047617molecular_functionfatty acyl-CoA hydrolase activity
A0072330biological_processmonocarboxylic acid biosynthetic process
A0140722biological_processmycophenolic acid biosynthetic process
B0005782cellular_componentperoxisomal matrix
B0016114biological_processterpenoid biosynthetic process
B0016787molecular_functionhydrolase activity
B0017000biological_processantibiotic biosynthetic process
B0047617molecular_functionfatty acyl-CoA hydrolase activity
B0072330biological_processmonocarboxylic acid biosynthetic process
B0140722biological_processmycophenolic acid biosynthetic process
C0005782cellular_componentperoxisomal matrix
C0016114biological_processterpenoid biosynthetic process
C0016787molecular_functionhydrolase activity
C0017000biological_processantibiotic biosynthetic process
C0047617molecular_functionfatty acyl-CoA hydrolase activity
C0072330biological_processmonocarboxylic acid biosynthetic process
C0140722biological_processmycophenolic acid biosynthetic process
D0005782cellular_componentperoxisomal matrix
D0016114biological_processterpenoid biosynthetic process
D0016787molecular_functionhydrolase activity
D0017000biological_processantibiotic biosynthetic process
D0047617molecular_functionfatty acyl-CoA hydrolase activity
D0072330biological_processmonocarboxylic acid biosynthetic process
D0140722biological_processmycophenolic acid biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues13
Detailsbinding site for residue MOA A 501
ChainResidue
AGLY59
AARG301
APRO304
APHE327
AHIS365
AVAL60
AALA139
APHE140
AGLN167
ASER169
APRO171
AILE183
AGLN265

site_idAC2
Number of Residues15
Detailsbinding site for residue MOA B 501
ChainResidue
BGLY59
BVAL60
BALA139
BPHE140
BLEU165
BGLN167
BPRO171
BALA182
BILE183
BGLN265
BARG301
BPHE327
BHIS365
BHOH662
BHOH775

site_idAC3
Number of Residues16
Detailsbinding site for residue MOA C 501
ChainResidue
CGLY59
CVAL60
CALA139
CPHE140
CLEU165
CGLN167
CPRO171
CALA182
CILE183
CGLN265
CARG301
CPRO304
CPHE327
CHIS365
CHOH649
CHOH750

site_idAC4
Number of Residues11
Detailsbinding site for residue MOA D 501
ChainResidue
DGLY59
DVAL60
DALA139
DPHE140
DGLN167
DPRO171
DGLN265
DARG301
DPRO304
DPHE327
DHIS365

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues752
DetailsRegion: {"description":"Abhydrolase domain","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"31209052","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"33843134","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsActive site: {"evidences":[{"source":"PubMed","id":"33843134","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31209052","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"33843134","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7DBL","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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