Structure of PDB 1o12 Chain B Binding Site BS01

Receptor Information

>1o12 Chain B (length=363) Species: 2336 (Thermotoga maritima)

MIVEKVLIVDPIDGEFTGDVEIEEGKIVKVEKRECIPRGVLMPGFVDPHI
HGVVGADTMNCDFSEMEEFLYSQGVTTFLATTVSTSLEKMKEILRKARDY
ILENPSTSLLGVHLEGPYISKEKKGAHSEKHIRPPSERELSEIDSPAKML
TFAPEIESSELLLRLVKRDIVLSAGHSIATFEEFMKFYKEGVKRITHFPN
GLKPLHHREIGITGAGLLLDDVKLELICDGVHLSREMVKLVYKVKKANGI
VLVTDSISAAGLKDGTTTLGDLVVKVKDGVPRLEDGTLAGSTLFFSQAVK
NFRKFTGCSITELAKVSSYNSCVELGLDDRGRIAEGTRADLVLLDEDLNV
VMTIKEGEVVFRS

Ligand information

• Ligand ID: FE
• InChI: InChI=1S/Fe/q+3
• InChIKey: VTLYFUHAOXGGBS-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  CACTVS 3.341
  OpenEye OEToolkits 1.5.0: [Fe+3]
• Formula: Fe
• Name: FE (III) ION
• DrugBank: DB13949
• PDB chain: 1o12 Chain B Residue 401

Receptor-Ligand Complex Structure

Structure summary

• PDB: 1o12 Crystal structure of N-acetylglucosamine-6-phosphate deacetylase (TM0814) from Thermotoga maritima at 2.5 A resolution
• Resolution: 2.5 Å
• Binding residue (original residue number in PDB): E115 H176 H197
• Binding residue (residue number reindexed from 1): E115 H176 H197
• 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

Biological Process

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

External links

• PDB: RCSB:1o12, PDBe:1o12, PDBj:1o12
• PDBsum: 1o12
• UniProt: Q9WZS1