Structure of PDB 6fv3 Chain D Binding Site BS02

Receptor Information

>6fv3 Chain D (length=350) Species: 246196 (Mycolicibacterium smegmatis MC2 155)

HMLLTADTVLTGTELLRPGWLEIASDRVVAVGAGAPPAQADRNLGAATVV
PGFVDTHLHGGGGGNFSAATDDETARAVALHRAHGSTTLVASLVTAGPED
LLRQVSGLARQVRAGLIDGIHLEGPWLSTLRCGAHQPVLMRDPDPGEIGR
VLDAGEGTVRMVTIAPERDGALAAIAQLVNAGVVAAVGHTEATYDQTRAA
IDAGATVGTHLFNAMRPIDRREPGPAVALTEDSRVTVEMIVDGVHVAPAI
YRHITQTVGPERLSLITDAMAATGMSSTATMEQVFRLAVAHCGLPRDDAL
SLAVRQACVNPARALGLPAAGLAAGARADLVVLDHDLAVTAVMRAGEWVV

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: 6fv3 Chain D Residue 402

Receptor-Ligand Complex Structure

Structure summary

• PDB: 6fv3 Structural and functional determination of homologs of theMycobacterium tuberculosis N-acetylglucosamine-6-phosphate deacetylase (NagA).
• Resolution: 2.58 Å
• Binding residue (original residue number in PDB): E122 H188 H209
• Binding residue (residue number reindexed from 1): E123 H189 H210
• Annotation score: 1

Enzymatic activity

• Enzyme Commision number: 3.5.1.25: N-acetylglucosamine-6-phosphate deacetylase.

Gene Ontology

Molecular Function

• GO:0008448 N-acetylglucosamine-6-phosphate deacetylase activity
• GO:0016787 hydrolase activity
• GO:0016810 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
• GO:0046872 metal ion binding
• GO:0047419 N-acetylgalactosamine-6-phosphate deacetylase activity

Biological Process

• GO:0006040 amino sugar metabolic process
• GO:0006044 N-acetylglucosamine metabolic process
• GO:0006046 N-acetylglucosamine catabolic process

External links

• PDB: RCSB:6fv3, PDBe:6fv3, PDBj:6fv3
• PDBsum: 6fv3
• PubMed: 29728457
• UniProt: A0QU89