Structure of PDB 4izw Chain A Binding Site BS03

Receptor Information

>4izw Chain A (length=262) Species: 501897 (Nesterenkonia sp. 10004)

GLVPRGSHMRIALMQHTARPLDPQHNLDLIDDAAARASEQGAQLLLTPLL
FGFGYVPSQICAQVSAEQVDAARSRLRGIARDRGIALVWSLPGPEGPEQR
GITAELADEHGEVLASYQKVQLYGPEEKAAFVPGEQPPPVLSWGGRQLSL
LVCYDVEFPEMVRAAAARGAQLVLVPTALAGDETSVPGILLPARAVENGI
TLAYANHCGPEGGLVFDGGSVVVGPAGQPLGELGVEPGLLVVDLPDADYL
QDRRAELHRNWL

Ligand information

• Ligand ID: FTM
• InChI: InChI=1S/C2H4FNO/c3-1-2(4)5/h1H2,(H2,4,5)
• InChIKey: FVTWJXMFYOXOKK-UHFFFAOYSA-N
• SMILES:
  ACDLabs 12.01: FCC(=O)N
  OpenEye OEToolkits 1.7.6: C(C(=O)N)F
  CACTVS 3.370: NC(=O)CF
• Formula: C2 H4 F N O
• Name: 2-fluoroacetamide
• ChEMBL: CHEMBL160811
• ZINC: ZINC000005177774
• PDB chain: 4izw Chain A Residue 304

Receptor-Ligand Complex Structure

Structure summary

• PDB: 4izw Covalent modifications of the active site cysteine occur as a result of mutating the glutamate of the catalytic triad in the amidase from Nesterenkonia sp.
• Resolution: 1.6 Å
• Binding residue (original residue number in PDB): V112 Q113 L114
• Binding residue (residue number reindexed from 1): V120 Q121 L122
• Annotation score: 1

Enzymatic activity

• Enzyme Commision number: 3.5.1.4: amidase.

Gene Ontology

Molecular Function

• GO:0004040 amidase activity
• GO:0016787 hydrolase activity
• GO:0043864 indoleacetamide hydrolase activity
• GO:0050126 N-carbamoylputrescine amidase activity

Biological Process

• GO:0033388 putrescine biosynthetic process from arginine

External links

• PDB: RCSB:4izw, PDBe:4izw, PDBj:4izw
• PDBsum: 4izw
• UniProt: D0VWZ1