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6LZH

Crystal structure of Alpha/beta hydrolase GrgF from Penicillium sp. sh18

Functional Information from GO Data
ChainGOidnamespacecontents
A0016740molecular_functiontransferase activity
A0017000biological_processantibiotic biosynthetic process
A0072330biological_processmonocarboxylic acid biosynthetic process
B0016740molecular_functiontransferase activity
B0017000biological_processantibiotic biosynthetic process
B0072330biological_processmonocarboxylic acid biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue NA A 301
ChainResidue
AASP262
AILE263
AHOH421
AHOH441
AHOH507
AHOH549

site_idAC2
Number of Residues5
Detailsbinding site for residue NA A 302
ChainResidue
AHOH535
AHOH566
ASER215
ATRP218
AHOH408

site_idAC3
Number of Residues6
Detailsbinding site for residue NA B 301
ChainResidue
BSER215
BTRP218
BHOH441
BHOH474
BHOH493
BHOH510

site_idAC4
Number of Residues5
Detailsbinding site for residue NA B 302
ChainResidue
AASN250
AGLU253
AHOH439
AHOH468
BASP166

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsActive site: {"evidences":[{"source":"PubMed","id":"32275405","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6LZH","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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