Structure of PDB 4pc8 Chain A Binding Site BS01

Receptor Information

>4pc8 Chain A (length=239) Species: 5702 (Trypanosoma brucei brucei)

MSKPQPIAAANWKSGSPDSLSELIDLFNSTSINHDVQCVVASTFVHLAMT
KERLSHPKFVIAALNAGNADALASLKDFGVNWIVLGHSERRWYYGETNEI
VADKVAAAVASGFMVIACIGETLQERESGRTAVVVLTQIAAIAKKLKKAD
WAKVVIAYEPVWAIGTGKVATPQQAQEAHALIRSWVSSKIGADVAGELRI
LYGGSVNGKNARTLYQQRDVNGFLAGLKPEFVDIIKATQ

Ligand information

• Ligand ID: GOA
• InChI: InChI=1S/C2H4O3/c3-1-2(4)5/h3H,1H2,(H,4,5)
• InChIKey: AEMRFAOFKBGASW-UHFFFAOYSA-N
• SMILES:
  ACDLabs 12.01: O=C(O)CO
  OpenEye OEToolkits 1.7.0: C(C(=O)O)O
  CACTVS 3.370: OCC(O)=O
• Formula: C2 H4 O3
• Name: GLYCOLIC ACID;
  HYDROXYACETIC ACID;
  HYDROXYETHANOIC ACID
• ChEMBL: CHEMBL252557
• DrugBank: DB03085
• ZINC: ZINC000004658557
• PDB chain: 4pc8 Chain A Residue 301

Receptor-Ligand Complex Structure

Structure summary

• PDB: 4pc8 Crystal structures of two monomeric triosephosphate isomerase variants identified via a directed-evolution protocol selecting for L-arabinose isomerase activity.
• Resolution: 1.55 Å
• Binding residue (original residue number in PDB): G173 S213
• Binding residue (residue number reindexed from 1): G165 S205
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): N11 K13 H95 E97 E167 G173 S213
• Catalytic site (residue number reindexed from 1): N11 K13 H87 E89 E159 G165 S205
• Enzyme Commision number: 5.3.1.1: triose-phosphate isomerase.

Gene Ontology

Molecular Function

• GO:0004807 triose-phosphate isomerase activity

Biological Process

• GO:0006096 glycolytic process

External links

• PDB: RCSB:4pc8, PDBe:4pc8, PDBj:4pc8
• PDBsum: 4pc8
• PubMed: 27303904
• UniProt: P04789|TPIS_TRYBB Triosephosphate isomerase, glycosomal