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3V1N

Crystal Structure of the H265Q mutant of a C-C hydrolase, BphD from Burkholderia xenovorans LB400, after exposure to 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 Residues13
DetailsBINDING SITE FOR RESIDUE MLA A 287
ChainResidue
AGLU34
AHOH297
AHOH356
AHOH425
AHOH443
ATHR35
AARG65
AASP102
AILE103
AASP104
AARG105
ASER180
AILE182

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE BEZ A 288
ChainResidue
AGLY41
AGLY42
ASER112
AMET113
AILE153
ALEU213
AVAL240

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE HPK A 289
ChainResidue
AHIS40
AGLY41
AALA46
AGLY47
ASER50
AASN51
ALEU176
ALEU181
ALEU186
AARG190
ATRP266
AHOH440
AHOH455

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AGLN265

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
ASER112

218853

PDB entries from 2024-04-24

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