Structure of PDB 2rhw Chain A

Receptor sequence

>2rhwA (length=283) Species: 266265 (Paraburkholderia xenovorans LB400)

LTESSTSKFVKINEKGFSDFNIHYNEAGNGETVIMLHGGGPGAGGWSNYY
RNVGPFVDAGYRVILKDSPGFNKSDAVVMDEQRGLVNARAVKGLMDALDI
DRAHLVGNAMGGATALNFALEYPDRIGKLILMGPGGLGPSMFAPMPMEGI
KLLFKLYAEPSYETLKQMLQVFLYDQSLITEELLQGRWEAIQRQPEHLKN
FLISAQKAPLSTWDVTARLGEIKAKTFITWGRDDRFVPLDHGLKLLWNID
DARLHVFSKCGHWAQWEHADEFNRLVIDFLRHA

3D structure

• PDB: 2rhw The Molecular Basis for Inhibition of BphD, a C-C Bond Hydrolase Involved in Polychlorinated Biphenyls Degradation: LARGE 3-SUBSTITUENTS PREVENT TAUTOMERIZATION.
• Chain: A
• Resolution: 1.57 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): G42 G43 G45 N111 A112 M113 R190 D237 H265 W266
• Catalytic site (residue number reindexed from 1): G39 G40 G42 N108 A109 M110 R187 D234 H262 W263
• 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	C0E	A	G41 G42 G43 A112 M113 G138 I153 F175 L213 F239 V240 H265	G38 G39 G40 A109 M110 G135 I150 F172 L210 F236 V237 H262

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

External links

• PDB: RCSB:2rhw, PDBe:2rhw, PDBj:2rhw
• PDBsum: 2rhw
• PubMed: 17932031
• UniProt: P47229|BPHD_PARXL 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase (Gene Name=bphD)