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3V1L

Crystal Structure of the S112A/H265Q mutant of a C-C hydrolase, BphD from Burkholderia xenovorans LB400

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0009056biological_processcatabolic process
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0016823molecular_functionhydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances
A0018771molecular_function2-hydroxy-6-oxonona-2,4-dienedioate hydrolase activity
A0018774molecular_function2,6-dioxo-6-phenylhexa-3-enoate hydrolase activity
A0046464biological_processacylglycerol catabolic process
A0047372molecular_functionmonoacylglycerol lipase activity
A0070980biological_processbiphenyl catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE MLA A 287
ChainResidue
AGLU34
AHOH305
AHOH410
AHOH427
ATHR35
AARG65
AILE103
AASP104
AARG105
ASER180
AILE182
AHOH293

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsSite: {"description":"Transition state stabilizer"}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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