Structure of PDB 2hjp Chain A

Receptor sequence
>2hjpA (length=283) Species: 218557 (Variovorax sp. Pal2) [Search protein sequence]
MTKNQALRAALDSGRLFTAMAAHNPLVAKLAEQAGFGGIWGSGFELSASY
AVPDANILSMSTHLEMMRAIASTVSIPLIADIDTGFGNAVNVHYVVPQYE
AAGASAIVMEDKTFPKDTQELVRIEEFQGKIAAATAARADRDFVVIARVE
ALIAGLGQQEAVRRGQAYEEAGADAILIHSRQKTPDEILAFVKSWPGKVP
LVLVPTAYPQLTEADIAALSKVGIVIYGNHAIRAAVGAVREVFARIRRDG
GIREVDAALPSVKEIIELQGDERMRAVEARYLK
3D structure
PDB2hjp Structure and Kinetics of Phosphonopyruvate Hydrolase from Voriovorax sp. Pal2: New Insight into the Divergence of Catalysis within the PEP Mutase/Isocitrate Lyase Superfamily
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) W40 S42 G43 F44 D54 D81 D83 V108 E110 K116 T118 R155 H186 V211
Catalytic site (residue number reindexed from 1) W40 S42 G43 F44 D54 D81 D83 V108 E110 K116 T118 R148 H179 V204
Enzyme Commision number 3.11.1.3: phosphonopyruvate 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 XYS A E32 S75 E32 S75
BS02 PPR A W40 S42 F44 D81 R155 H186 R188 W40 S42 F44 D81 R148 H179 R181
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0016787 hydrolase activity
GO:0033978 phosphonopyruvate hydrolase activity
GO:0046872 metal ion binding

View graph for
Molecular Function
External links
PDB RCSB:2hjp, PDBe:2hjp, PDBj:2hjp
PDBsum2hjp
PubMed16981709
UniProtQ84G06|PPHA_VARSP Phosphonopyruvate hydrolase (Gene Name=pphA)

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