Structure of PDB 2og1 Chain A

Receptor sequence
>2og1A (length=285) Species: 266265 (Paraburkholderia xenovorans LB400) [Search protein sequence]
TALTESSTSKFVKINEKGFSDFNIHYNEAGNGETVIMLHGGGPGAGGWSN
YYRNVGPFVDAGYRVILKDSPGFNKSDAVVMDEQRGLVNARAVKGLMDAL
DIDRAHLVGNSMGGATALNFALEYPDRIGKLILMGPGGLGPSMFAPMPME
GIKLLFKLYAEPSYETLKQMLQVFLYDQSLITEELLQGRWEAIQRQPEHL
KNFLISAQKAPLSTWDVTARLGEIKAKTFITWGRDDRFVPLDHGLKLLWN
IDDARLHVFSKCGHWAQWEHADEFNRLVIDFLRHA
3D structure
PDB2og1 Kinetic and structural insight into the mechanism of BphD, a C-C bond hydrolase from the biphenyl degradation pathway
ChainA
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G42 G43 G45 N111 S112 M113 L156 R190 A208 D237 H265 W266
Catalytic site (residue number reindexed from 1) G41 G42 G44 N110 S111 M112 L155 R189 A207 D236 H264 W265
Enzyme Commision number 3.7.1.8: 2,6-dioxo-6-phenylhexa-3-enoate hydrolase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 GOL A Y53 E185 Y52 E184
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0016787 hydrolase activity
GO:0016823 hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances
GO:0018771 2-hydroxy-6-oxonona-2,4-dienedioate hydrolase activity
GO:0018774 2,6-dioxo-6-phenylhexa-3-enoate hydrolase activity
Biological Process
GO:0009056 catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2og1, PDBe:2og1, PDBj:2og1
PDBsum2og1
PubMed16964968
UniProtP47229|BPHD_PARXL 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase (Gene Name=bphD)

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