Structure of PDB 2ish Chain A Binding Site BS01

Receptor Information

>2ish Chain A (length=416) Species: 1491 (Clostridium botulinum)

PFVNKQFNYKDPVNGVDIAYIKIPNAGQMQPVKAFKIHNKIWVIPERDTF
TNPEEGDLNPPPEAKQVPVSYYDSTYLSTDNEKDNYLKGVTKLFERIYST
DLGRMLLTSIVRGIPFWGGSTIDTELKVIDTNCINVIQPDGSYRSEELNL
VIIGPSADIIQFECKSFGHEVLNLTRNGYGSTQYIRFSPDFTFGFEESLE
VDTNPLLGAGKFATDPAVTLAHELIHAGHRLYGIAINPNRVFKVNTNAYY
EMSGLEVSFEELRTFGGHDAKFIDSLQENEFRLYYYNKFKDIASTLNKAK
SIVGTTASLQYMKNVFKEKYLLSEDTSGKFSVDKLKFDKLYKMLTEIYTE
DNFVKFFKVLNRKTYLNFDKAVFKINIVPKVNYTIYDGFNLRNTNLAANF
NGQNTEINNMNFTKLK

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: 2ish Chain A Residue 500

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2ish Inhibition of metalloprotease botulinum serotype A from a pseudo-peptide binding mode to a small molecule that is active in primary neurons.
• Resolution: 2.0 Å
• Binding residue (original residue number in PDB): H223 H227 E262
• Binding residue (residue number reindexed from 1): H222 H226 E261
• Annotation score: 4

Enzymatic activity

• Catalytic site (original residue number in PDB): H223 E224 H227 E262 R363
• Catalytic site (residue number reindexed from 1): H222 E223 H226 E261 R362
• Enzyme Commision number: 3.4.24.69: bontoxilysin.

Gene Ontology

Molecular Function

• GO:0004222 metalloendopeptidase activity
• GO:0008270 zinc ion binding

Biological Process

• GO:0006508 proteolysis

External links

• PDB: RCSB:2ish, PDBe:2ish, PDBj:2ish
• PDBsum: 2ish
• PubMed: 17092934
• UniProt: Q7B8V4