Structure of PDB 5a65 Chain B Binding Site BS04

Receptor Information

>5a65 Chain B (length=197) Species: 10090 (Mus musculus)

GAMTQGLIEVERKFAPGPDTEERLQELGATLEHRVTFRDTYYDTSELSLM
LSDHWLRQREGSGWELKCPHNEYVEVTSEAAIVAQLFELLPAGVAAVLGS
LKLQEVASFITTRSSWKLALSEPQLTIDLDSADFGYAVGEVEAMVHEKAE
VPAALEKIITVSSMLGVPAQEEAPAKLMVYLQRFRPLDYQRLLEAAS

Ligand information

• Ligand ID: PO4
• InChI: InChI=1S/H3O4P/c1-5(2,3)4/h(H3,1,2,3,4)/p-3
• InChIKey: NBIIXXVUZAFLBC-UHFFFAOYSA-K
• SMILES:
  CACTVS 3.341: [O-][P]([O-])([O-])=O
  ACDLabs 10.04: [O-]P([O-])([O-])=O
  OpenEye OEToolkits 1.5.0: [O-]P(=O)([O-])[O-]
• Formula: O4 P
• Name: PHOSPHATE ION
• DrugBank: DB14523
• PDB chain: 5a65 Chain B Residue 1001

Receptor-Ligand Complex Structure

Structure summary

• PDB: 5a65 Structural Determinants for Substrate Binding and Catalysis in Triphosphate Tunnel Metalloenzymes.
• Resolution: 1.98 Å
• Binding residue (original residue number in PDB): R57 R125 E159
• Binding residue (residue number reindexed from 1): R59 R113 E142
• Annotation score: 1

Enzymatic activity

• Enzyme Commision number: 3.6.1.28: thiamine-triphosphatase.

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0016462 pyrophosphatase activity
• GO:0016787 hydrolase activity
• GO:0046872 metal ion binding
• GO:0050333 thiamine triphosphate phosphatase activity

Biological Process

• GO:0006772 thiamine metabolic process
• GO:0009229 thiamine diphosphate biosynthetic process
• GO:0016311 dephosphorylation
• GO:0042357 thiamine diphosphate metabolic process

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol

External links

• PDB: RCSB:5a65, PDBe:5a65, PDBj:5a65
• PDBsum: 5a65
• PubMed: 26221030
• UniProt: Q8JZL3|THTPA_MOUSE Thiamine-triphosphatase (Gene Name=Thtpa)