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2PU7

Crystal Structure of S112A/H265A double mutant of a C-C hydrolase, BphD, from Burkholderia xenovorans LB400

Functional Information from GO Data
ChainGOidnamespacecontents
A0009056biological_processcatabolic process
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
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 287
ChainResidue
AARG105
AMLI288
AHOH361
AHOH362

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MLI A 288
ChainResidue
AARG105
ASER180
ANA287
AGLU34
ATHR35
AARG65
AILE103
AASP104

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE MLI A 289
ChainResidue
AGLY41
AGLY43
AASN111
AALA112
APHE175
AARG190
AALA265
ATRP266
AHOH329
AHOH355

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AALA265

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

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PDB entries from 2024-07-24

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