Structure of PDB 4cz1 Chain B Binding Site BS01

Receptor Information

>4cz1 Chain B (length=206) Species: 198094 (Bacillus anthracis str. Ames)

SKWIDISQPLNNDIATWPGDTPFSYEVLWSKEESGSVNVGKLTMSIHTGT
HIDAPFHFDNDGKKVLDLDIQVYVGPTRIIDVSNLESIGKKELEKFHLEG
VERLLLRTSSHGKANEFPDIIPHLRADIAPFLSEKGIRLIGVDVPSVDPL
DDKELAAHHQLFKHSIHILENVVLDHVADGDYELIALPLALSDADGSPVR
AVIRPI

Ligand information

• Ligand ID: VNJ
• InChI: InChI=1S/C8H9NO/c1-6(10)7-4-2-3-5-8(7)9/h2-5H,9H2,1H3
• InChIKey: GTDQGKWDWVUKTI-UHFFFAOYSA-N
• SMILES:
  ACDLabs 12.01: O=C(c1ccccc1N)C
  CACTVS 3.385
  OpenEye OEToolkits 1.7.6: CC(=O)c1ccccc1N
• Formula: C8 H9 N O
• Name: 2-aminoacetophenone
• ChEMBL: CHEMBL2251601
• ZINC: ZINC000000164490
• PDB chain: 4cz1 Chain A Residue 501

Receptor-Ligand Complex Structure

Structure summary

• PDB: 4cz1 Structure of Bacterial Kynurenine Formamidase Reveals a Crowded Binuclear-Zinc Catalytic Site Primed to Generate a Potent Nucleophile.
• Resolution: 2.24 Å
• Binding residue (original residue number in PDB): V40 V42
• Binding residue (residue number reindexed from 1): V37 V39
• Annotation score: 1

Enzymatic activity

• Enzyme Commision number: 3.5.1.9: arylformamidase.

Gene Ontology

Molecular Function

• GO:0004061 arylformamidase activity
• GO:0004328 formamidase activity
• GO:0008270 zinc ion binding
• GO:0016787 hydrolase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0006569 tryptophan catabolic process
• GO:0019441 tryptophan catabolic process to kynurenine
• GO:0043420 anthranilate metabolic process

External links

• PDB: RCSB:4cz1, PDBe:4cz1, PDBj:4cz1
• PDBsum: 4cz1
• PubMed: 24942958
• UniProt: Q81PP9|KYNB_BACAN Kynurenine formamidase (Gene Name=kynB)