Structure of PDB 1lvu Chain A Binding Site BS01

Receptor Information

>1lvu Chain A (length=272) Species: 9913 (Bos taurus)

QNGYTYEDYQDTAKWLLSHTEQRPQVAVICGSGLGGLVNKLTQAQTFDYS
EIPNFPESTVPGHAGRLVFGILNGRACVMMQGRFHMYEGYPFWKVTFPVR
VFRLLGVETLVVTNAAGGLNPNFEVGDIMLIRDHINLPGFSGQNPLRGPN
EERFGVRFPAMSDAYDRDMRQKAHSTWKQMGEQRELQEGTYVMLGGPNFE
TVAECRLLRNLGADAVGMSTVPEVIVARHCGLRVFGFSLITNKVIMDYEE
AGKQAAQKLEQFVSLLMASIPV

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: 1lvu Chain A Residue 8001

Receptor-Ligand Complex Structure

Structure summary

• PDB: 1lvu Crystal structure of calf spleen purine nucleoside phosphorylase with two full trimers in the asymmetric unit: important implications for the mechanism of catalysis
• Resolution: 2.05 Å
• Binding residue (original residue number in PDB): S51 E58
• Binding residue (residue number reindexed from 1): S50 E57
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): S33 H64 Y88 A116 M219 S220
• Catalytic site (residue number reindexed from 1): S32 H63 Y87 A115 M218 S219
• Enzyme Commision number: 2.4.2.1: purine-nucleoside phosphorylase.

Gene Ontology

Molecular Function

• GO:0003824 catalytic activity
• GO:0004731 purine-nucleoside phosphorylase activity
• GO:0016757 glycosyltransferase activity
• GO:0016763 pentosyltransferase activity
• GO:0047975 guanosine phosphorylase activity

Biological Process

• GO:0006139 nucleobase-containing compound metabolic process
• GO:0006166 purine ribonucleoside salvage
• GO:0009116 nucleoside metabolic process

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:1lvu, PDBe:1lvu, PDBj:1lvu
• PDBsum: 1lvu
• PubMed: 15342253
• UniProt: P55859|PNPH_BOVIN Purine nucleoside phosphorylase (Gene Name=PNP)