Structure of PDB 2ff1 Chain B Binding Site BS01

Receptor Information

>2ff1 Chain B (length=316) Species: 5699 (Trypanosoma vivax)

SAKNVVLDHDGNLDDFVAMVLLASNTEKVRLIGALCTDADCFVENGFNVT
GKIMCLMHNNMNLPLFPIGKSAATAVNPFPKEWRCLAKNMDDMPILNIPE
NVELWDKIKAENEKYEGQQLLADLVMNSEEKVTICVTGPLSNVAWCIDKY
GEKFTSKVEECVIMGGAVDVRGNVFLPSTDGTAEWNIYWDPASAKTVFGC
PGLRRIMFSLDSTNTVPVRSPYVQRFGEQTNFLLSILVGTMWAMGYYAWD
ALTAAYVVDQKVANVDPVPIDVVVDKQPNEGATVRTDAENYPLTFVARNP
EAEFFLDMLLRSARAC

Ligand information

• Ligand ID: CA
• InChI: InChI=1S/Ca/q+2
• InChIKey: BHPQYMZQTOCNFJ-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.341: [Ca++]
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Ca+2]
• Formula: Ca
• Name: CALCIUM ION
• DrugBank: DB14577
• PDB chain: 2ff1 Chain B Residue 602

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2ff1 Transition-state Complex of the Purine-specific Nucleoside Hydrolase of T.vivax: Enzyme Conformational Changes and Implications for Catalysis.
• Resolution: 2.07 Å
• Binding residue (original residue number in PDB): D10 D15 T137 D261
• Binding residue (residue number reindexed from 1): D10 D15 T137 D250
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): D10 D15 D40 W83 T137 W185 N186 W260 D261
• Catalytic site (residue number reindexed from 1): D10 D15 D40 W83 T137 W185 N186 W249 D250
• Enzyme Commision number: 3.2.2.1: purine nucleosidase.

Gene Ontology

Molecular Function

• GO:0016798 hydrolase activity, acting on glycosyl bonds
• GO:0016799 hydrolase activity, hydrolyzing N-glycosyl compounds
• GO:0046872 metal ion binding

Biological Process

• GO:0006139 nucleobase-containing compound metabolic process

External links

• PDB: RCSB:2ff1, PDBe:2ff1, PDBj:2ff1
• PDBsum: 2ff1
• PubMed: 16630632
• UniProt: Q9GPQ4