Structure of PDB 4c5y Chain A Binding Site BS01

Receptor Information

>4c5y Chain A (length=436) Species: 5061 (Aspergillus niger)

DEAKVTIIYAGLLIPGDGEPLRNAALVISDKIIAFVGSEADIPKKYLRST
QSTHRVPVLMPGLWDCHMHFGGDDDYYNDYTSGLATHPASSGARLARGCW
EALQNGYTSYRDLAGYGCEVAKAINDGTIVGPNVYSSGAALSQTAGHGDI
FALPAGEVLGSYGVMNPRPGYWGAGPLCIADGVEEVRRAVRLQIRRGAKV
IKVMASGGVMSRDDNPNFAQFSPEELKVIVEEAARQNRIVSAHVHGKAGI
MAAIKAGCKSLEHVSYADEEVWELMKEKGILYVATRSVIEIFLASNGEGL
VKESWAKLQALADSHLKAYQGAIKAGVTIALGTDTAPGGPTALELQFAVE
RGGMTPLEAIKAATANAPLSVGPQAPLTGQLREGYEADVIALEENPLEDI
KVFQEPKAVTHVWKGGKLFKGPGIGPWGEDARNPFL

Ligand information

• Ligand ID: ZN
• InChI: InChI=1S/Zn/q+2
• InChIKey: PTFCDOFLOPIGGS-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.341: [Zn++]
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Zn+2]
• Formula: Zn
• Name: ZINC ION
• ChEMBL: CHEMBL1236970
• DrugBank: DB14532
• PDB chain: 4c5y Chain A Residue 500

Receptor-Ligand Complex Structure

Structure summary

• PDB: 4c5y Structural and Functional Characterization of Ochratoxinase, a Novel Mycotoxin Degrading Enzyme.
• Resolution: 3.0 Å
• Binding residue (original residue number in PDB): H111 H113 K246
• Binding residue (residue number reindexed from 1): H67 H69 K202
• Annotation score: 1

Enzymatic activity

• Enzyme Commision number: 3.4.17.-

Gene Ontology

Molecular Function

• GO:0004180 carboxypeptidase activity
• GO:0008237 metallopeptidase activity
• GO:0016787 hydrolase activity
• GO:0016810 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
• GO:0046872 metal ion binding

Biological Process

• GO:0006508 proteolysis
• GO:1900817 ochratoxin A catabolic process

Cellular Component

• GO:0005575 cellular_component
• GO:0005576 extracellular region

External links

• PDB: RCSB:4c5y, PDBe:4c5y, PDBj:4c5y
• PDBsum: 4c5y
• PubMed: 24947135
• UniProt: A2R2V4|OTASE_ASPNC Ochratoxinase (Gene Name=Am2)