Structure of PDB 2puj Chain A

Receptor sequence

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

LTESSTSKFVKINEKGFSDFNIHYNEAGNGETVIMLHGGGPGAGGWSNYY
RNVGPFVDAGYRVILKDSPGFNKSDAVVMDEQRGLVNARAVKGLMDALDI
DRAHLVGNAMGGATALNFALEYPDRIGKLILMGPGGLGPSMFAPMPMEGI
KLLFKLYAEPSYETLKQMLQVFLYDQSLITEELLQGRWEAIQRQPEHLKN
FLISAQKAPLSTWDVTARLGEIKAKTFITWGRDDRFVPLDHGLKLLWNID
DARLHVFSKCGAWAQWEHADEFNRLVIDFLRHA

3D structure

• PDB: 2puj The Tautomeric Half-reaction of BphD, a C-C Bond Hydrolase: KINETIC AND STRUCTURAL EVIDENCE SUPPORTING A KEY ROLE FOR HISTIDINE 265 OF THE CATALYTIC TRIAD.
• Chain: A
• Resolution: 1.57 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): G42 G43 G45 N111 A112 M113 R190 D237 A265 W266
• Catalytic site (residue number reindexed from 1): G39 G40 G42 N108 A109 M110 R187 D234 A262 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	HPZ	A	G41 G42 G43 A112 M113 G138 I153 L156 F175 R190 V240	G38 G39 G40 A109 M110 G135 I150 L153 F172 R187 V237

Gene Ontology

Molecular Function

• 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:2puj, PDBe:2puj, PDBj:2puj
• PDBsum: 2puj
• PubMed: 17442675
• UniProt: P47229|BPHD_PARXL 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase (Gene Name=bphD)