Structure of PDB 1lv8 Chain A Binding Site BS01
Receptor Information
>1lv8 Chain A (length=265) Species:
9913
(Bos taurus) [
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NGYTYEDYQDTAKWLLSHTEQRPQVAVICGSGLGGLVNKLTQAQTFDYSE
IPNFPESTVPGHAGRLVFGILNGRACVMMQGRFHMYEGYPFWKVTFPVRV
FRLLGVETLVVTNAAGGLNPNFEVGDIMLIRDHINLPGFSGQNPLRGPNE
ERFGVRFPAMSDAYDRDMRQKAHSTWKQMGEQRELQEGTYVMLGGPNFET
VAECRLLRNLGADAVGMSTVPEVIVARHCGLRVFGFSLITNKVIMDQAAQ
KLEQFVSLLMASIPV
Ligand information
Ligand ID
CA
InChI
InChI=1S/Ca/q+2
InChIKey
BHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Ca+2]
Formula
Ca
Name
CALCIUM ION
ChEMBL
DrugBank
DB14577
ZINC
PDB chain
1lv8 Chain A Residue 7002 [
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Receptor-Ligand Complex Structure
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PDB
1lv8
Crystal structure of calf spleen purine nucleoside phosphorylase with two full trimers in the asymmetric unit: important implications for the mechanism of catalysis
Resolution
2.3 Å
Binding residue
(original residue number in PDB)
S51 E58
Binding residue
(residue number reindexed from 1)
S49 E56
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)
S31 H62 Y86 A114 M217 S218
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
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:1lv8
,
PDBe:1lv8
,
PDBj:1lv8
PDBsum
1lv8
PubMed
15342253
UniProt
P55859
|PNPH_BOVIN Purine nucleoside phosphorylase (Gene Name=PNP)
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