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2PUH

Crystal Structure of the S112A mutant of a C-C hydrolase, BphD from Burkholderia xenovorans LB400, in complex with its substrate HOPDA

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
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
A0019439biological_processobsolete aromatic compound catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA A 287
ChainResidue
AARG105
AMLI288
AHOH392

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE MLI A 288
ChainResidue
AILE182
ANA287
AHOH339
ATHR35
AARG65
AILE103
AASP104
AARG105
ASER180

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE HPK A 289
ChainResidue
AGLY42
AGLY43
AASN51
AASN111
AALA112
AMET113
AILE153
APHE175
AARG190
ALEU213
ATRP216
AVAL240
AHIS265
ATRP266

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AHIS265

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING:
ChainResidueDetails
AGLY42
AASN51
AASN111
ASER180
AARG190
ATRP266

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Transition state stabilizer
ChainResidueDetails
AALA112

218853

PDB entries from 2024-04-24

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