Structure of PDB 5vgv Chain A Binding Site BS01

Receptor Information

>5vgv Chain A (length=421) Species: 1491 (Clostridium botulinum)

QFVNKQFNYKDPVNGVDIAYIKIPNVGQMQPVKAFKIHNKIWVIPERDTF
TNPEEGDLNPPPEAKQVPVSYYDSTYLSTDNEKDNYLKGVTKLFERIYST
DLGRMLLTSIVRGIPFWGGSTIDTELKVIDTNCINVIQPDGSYRSEELNL
VIIGPSADIIQFECKSFGHEVLNLTRNGYGSTQYIRFSPDFTFGFEESLE
VDTNPLLGAGKFATDPAVTLAHELIHAGHRLYGIAINPNRVFKVNTNAYY
EMSGLEVSFEELRTFGGHDAKFIDSLQENEFRLYYYNKFKDIASTLNKAK
SIVGTTASLQYMKNVFKEKYLLSEDTSGKFSVDKLKFDKLYKMLTEIYTE
DNFVKFFKVLNRKTYLNFDKAVFKINIVPKVNYTIYDGFNLRNTNLAANF
NGQNTEINNMNFTKLKNFTGL

Ligand information

• Ligand ID: CU
• InChI: InChI=1S/Cu/q+2
• InChIKey: JPVYNHNXODAKFH-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Cu+2]
  CACTVS 3.341: [Cu++]
• Formula: Cu
• Name: COPPER (II) ION
• DrugBank: DB14552
• PDB chain: 5vgv Chain A Residue 502

Receptor-Ligand Complex Structure

Structure summary

• PDB: 5vgv Metal Ions Effectively Ablate the Action of Botulinum Neurotoxin A.
• Resolution: 2.6 Å
• Binding residue (original residue number in PDB): H223 H227 E262
• Binding residue (residue number reindexed from 1): H222 H226 E261
• Annotation score: 3

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:5vgv, PDBe:5vgv, PDBj:5vgv
• PDBsum: 5vgv
• PubMed: 28475321
• UniProt: P0DPI1|BXA1_CLOBH Botulinum neurotoxin type A (Gene Name=botA)