Structure of PDB 2ock Chain A

Receptor sequence
>2ockA (length=254) Species: 9606 (Homo sapiens) [Search protein sequence]
SVTSAKVAVNGVQLHYQQTGEGDHAVLLLPGMLGSGETDFGPQLKNLNKK
LFTVVAWDPRGYGHSRPPDRDFPADFFERDAKDAVDLMKALKFKKVSLLG
WSNGGITALIAAAKYPSYIHKMVIWGANAYVTDEDSMIYEGIRDVSKWSE
RTRKPLEALYGYDYFARTCEKWVDGIRQFKHLPDGNICRHLLPRVQCPAL
IVHGEKDPLVPRFHADFIHKHVKGSRLHLMPEGKHNLHLRFADEFNKLAE
DFLQ
3D structure
PDB2ock Molecular basis of prodrug activation by human valacyclovirase, an alpha-amino acid ester hydrolase.
ChainA
Resolution1.85 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S122
Catalytic site (residue number reindexed from 1) S102
Enzyme Commision number 3.1.-.-
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 MN A H35 E57 D78 H84 H15 E37 D58 H64
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
GO:0047658 alpha-amino-acid esterase activity
Biological Process
GO:0006520 amino acid metabolic process
GO:0006805 xenobiotic metabolic process
GO:0009636 response to toxic substance
Cellular Component
GO:0005739 mitochondrion
GO:0005741 mitochondrial outer membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2ock, PDBe:2ock, PDBj:2ock
PDBsum2ock
PubMed18256025
UniProtQ86WA6|BPHL_HUMAN Valacyclovir hydrolase (Gene Name=BPHL)

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