Structure of PDB 2ocg Chain A Binding Site BS01

Receptor Information

>2ocg Chain A (length=254) Species: 9606 (Homo sapiens)

SVTSAKVAVNGVQLHYQQTGEGDHAVLLLPGMLGSGETDFGPQLKNLNKK
LFTVVAWDPRGYGHSRPPDRDFPADFFERDAKDAVDLMKALKFKKVSLLG
WSDGGITALIAAAKYPSYIHKMVIWGANAYVTDEDSMIYEGIRDVSKWSE
RTRKPLEALYGYDYFARTCEKWVDGIRQFKHLPDGNICRHLLPRVQCPAL
IVHGEKDPLVPRFHADFIHKHVKGSRLHLMPEGKHNLHLRFADEFNKLAE
DFLQ

Ligand information

• Ligand ID: MN
• InChI: InChI=1S/Mn/q+2
• InChIKey: WAEMQWOKJMHJLA-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Mn+2]
  CACTVS 3.341: [Mn++]
• Formula: Mn
• Name: MANGANESE (II) ION
• DrugBank: DB06757
• PDB chain: 2ocg Chain A Residue 401

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2ocg Molecular basis of prodrug activation by human valacyclovirase, an alpha-amino acid ester hydrolase.
• Resolution: 1.75 Å
• Binding residue (original residue number in PDB): H35 E57 D78 H84
• Binding residue (residue number reindexed from 1): H15 E37 D58 H64
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): S122
• Catalytic site (residue number reindexed from 1): S102
• Enzyme Commision number: 3.1.-.-

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

External links

• PDB: RCSB:2ocg, PDBe:2ocg, PDBj:2ocg
• PDBsum: 2ocg
• PubMed: 18256025
• UniProt: Q86WA6|BPHL_HUMAN Valacyclovir hydrolase (Gene Name=BPHL)