Structure of PDB 1p52 Chain A

Receptor sequence
>1p52A (length=356) Species: 6850 (Limulus polyphemus) [Search protein sequence]
VDQATLDKLEAGFKKLQEASDCKSLLKKHLTKDVFDSIKNKKTGMGATLL
DVIQSGVENLDSGVGIYAPDAESYRTFGPLFDPIIDDYHGGFKLTDKHPP
KQWGDINTLVDLDPAGQFIISTRVRCGRSLQGYPFNPCLTAEQYKEMEEK
VSSTLSSMEDELKGTYYPLTGMSKATQQQLIDDHFLFKEGDRFLQTANAC
RYWPTGRGIFHNDAKTFLVWVNEEDHLRIISMQKGGDLKTVYKRLVTAVD
NIESKLPFSHDDRFGFLTFCPTNLGTTMRASVHIQLPKLAKDRKVLEDIA
SKFNLQVRGTRGDHTESEGGVYDISNKRRLGLTEYQAVREMQDGILEMIK
MEKAAA
3D structure
PDB1p52 The putative catalytic bases have, at most, an accessory role in the mechanism of arginine kinase.
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R126 E225 R229 C271 T273 R280 R309 D314
Catalytic site (residue number reindexed from 1) R125 E224 R228 C270 T272 R279 R308 D313
Enzyme Commision number 2.7.3.3: arginine kinase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ADP A S122 R124 R126 H185 W221 R229 M233 R280 S282 V283 H284 R309 G313 S121 R123 R125 H184 W220 R228 M232 R279 S281 V282 H283 R308 G312
BS02 DAR A S63 G64 V65 Y68 E225 C271 D314 H315 S62 G63 V64 Y67 E224 C270 D313 H314
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:1p52, PDBe:1p52, PDBj:1p52
PDBsum1p52
PubMed12732621
UniProtP51541|KARG_LIMPO Arginine kinase

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