Structure of PDB 1aw1 Chain H Binding Site BS01

Receptor Information

>1aw1 Chain H (length=254) Species: 90736 (Moritella marina)

RHPVVMGNWKLNGSKEMVVDLLNGLNAELEGVTGVDVAVAPPALFVDLAE
RTLTEAGSAIILGAQNTDLNNSGAFTGDMSPAMLKEFGATHIIIGHSERR
EYHAESDEFVAKKFAFLKENGLTPVLCIGESDAQNEAGETMAVCARQLDA
VINTQGVEALEGAIIAYEPIWAIGTGKAATAEDAQRIHAQIRAHIAEKSE
AVAKNVVIQYGGSVKPENAAAYFAQPDIDGALVGGAALDAKSFAAIAKAA
AEAK

Ligand information

• Ligand ID: PGA
• InChI: InChI=1S/C2H5O6P/c3-2(4)1-8-9(5,6)7/h1H2,(H,3,4)(H2,5,6,7)
• InChIKey: ASCFNMCAHFUBCO-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.341: OC(=O)CO[P](O)(O)=O
  OpenEye OEToolkits 1.5.0: C(C(=O)O)OP(=O)(O)O
  ACDLabs 10.04: O=P(O)(O)OCC(=O)O
• Formula: C2 H5 O6 P
• Name: 2-PHOSPHOGLYCOLIC ACID
• ChEMBL: CHEMBL47181
• DrugBank: DB02726
• ZINC: ZINC000003869735
• PDB chain: 1aw1 Chain H Residue 290

Receptor-Ligand Complex Structure

Structure summary

• PDB: 1aw1 Triose-phosphate isomerase (TIM) of the psychrophilic bacterium Vibrio marinus. Kinetic and structural properties.
• Resolution: 2.7 Å
• Binding residue (original residue number in PDB): K11 H97 E169 I174 G175 G213 S214 L233 G235
• Binding residue (residue number reindexed from 1): K10 H96 E168 I173 G174 G212 S213 L232 G234
• Annotation score: 2

Enzymatic activity

• Catalytic site (original residue number in PDB): N9 K11 H97 E99 E169 G175 S214
• Catalytic site (residue number reindexed from 1): N8 K10 H96 E98 E168 G174 S213
• Enzyme Commision number: 5.3.1.1: triose-phosphate isomerase.

Gene Ontology

Molecular Function

• GO:0004807 triose-phosphate isomerase activity
• GO:0016853 isomerase activity

Biological Process

• GO:0006094 gluconeogenesis
• GO:0006096 glycolytic process
• GO:0019563 glycerol catabolic process
• GO:0046166 glyceraldehyde-3-phosphate biosynthetic process

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol

External links

• PDB: RCSB:1aw1, PDBe:1aw1, PDBj:1aw1
• PDBsum: 1aw1
• PubMed: 9442062
• UniProt: P50921|TPIS_MORMI Triosephosphate isomerase (Gene Name=tpiA)