Structure of PDB 1bg0 Chain A Binding Site BS02
Receptor Information
>1bg0 Chain A (length=356) Species:
6850
(Limulus polyphemus) [
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VDQATLDKLEAGFKKLQEASDCKSLLKKHLTKDVFDSIKNKKTGMGATLL
DVIQSGVENLDSGVGIYAPDAESYRTFGPLFDPIIDDYHGGFKLTDKHPP
KQWGDINTLVGLDPAGQFIISTRVRCGRSLQGYPFNPCLTAEQYKEMEEK
VSSTLSSMEDELKGTYYPLTGMSKATQQQLIDDHFLFKEGDRFLQTANAC
RYWPTGRGIFHNDAKTFLVWVNEEDHLRIISMQKGGDLKTVYKRLVTAVD
NIESKLPFSHDDRFGFLTFCPTNLGTTMRASVHIQLPKLAKDRKVLEDIA
SKFNLQVRGTRGEHTESEGGVYDISNKRRLGLTEYQAVREMQDGILEMIK
MEKAAA
Ligand information
Ligand ID
NO3
InChI
InChI=1S/NO3/c2-1(3)4/q-1
InChIKey
NHNBFGGVMKEFGY-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
CACTVS 3.341
[O-][N+]([O-])=O
OpenEye OEToolkits 1.5.0
[N+](=O)([O-])[O-]
Formula
N O3
Name
NITRATE ION
ChEMBL
CHEMBL186200
DrugBank
DB14049
ZINC
PDB chain
1bg0 Chain A Residue 401 [
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Receptor-Ligand Complex Structure
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PDB
1bg0
Transition state structure of arginine kinase: implications for catalysis of bimolecular reactions.
Resolution
1.86 Å
Binding residue
(original residue number in PDB)
R126 R229 R309 E314
Binding residue
(residue number reindexed from 1)
R125 R228 R308 E313
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
R126 E225 R229 C271 T273 R280 R309 E314
Catalytic site (residue number reindexed from 1)
R125 E224 R228 C270 T272 R279 R308 E313
Enzyme Commision number
2.7.3.3
: arginine kinase.
Gene Ontology
Molecular Function
GO:0003824
catalytic activity
GO:0004054
arginine kinase activity
GO:0004111
creatine kinase activity
GO:0005524
ATP binding
GO:0016301
kinase activity
GO:0016772
transferase activity, transferring phosphorus-containing groups
Biological Process
GO:0016310
phosphorylation
GO:0046314
phosphocreatine biosynthetic 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:1bg0
,
PDBe:1bg0
,
PDBj:1bg0
PDBsum
1bg0
PubMed
9671698
UniProt
P51541
|KARG_LIMPO Arginine kinase
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