Structure of PDB 1bg0 Chain A

Receptor sequence

>1bg0A (length=356) Species: 6850 (Limulus polyphemus)

VDQATLDKLEAGFKKLQEASDCKSLLKKHLTKDVFDSIKNKKTGMGATLL
DVIQSGVENLDSGVGIYAPDAESYRTFGPLFDPIIDDYHGGFKLTDKHPP
KQWGDINTLVGLDPAGQFIISTRVRCGRSLQGYPFNPCLTAEQYKEMEEK
VSSTLSSMEDELKGTYYPLTGMSKATQQQLIDDHFLFKEGDRFLQTANAC
RYWPTGRGIFHNDAKTFLVWVNEEDHLRIISMQKGGDLKTVYKRLVTAVD
NIESKLPFSHDDRFGFLTFCPTNLGTTMRASVHIQLPKLAKDRKVLEDIA
SKFNLQVRGTRGEHTESEGGVYDISNKRRLGLTEYQAVREMQDGILEMIK
MEKAAA

3D structure

• PDB: 1bg0 Transition state structure of arginine kinase: implications for catalysis of bimolecular reactions.
• Chain: A
• Resolution: 1.86 Å

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.

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	NO3	A	G112 D114 P115 G237 D238	G111 D113 P114 G236 D237
BS02	NO3	A	R126 R229 R309 E314	R125 R228 R308 E313
BS03	ADP	A	S122 R124 R126 H185 W221 R229 R280 S282 V283 H284 R309 R312 G313 D324	S121 R123 R125 H184 W220 R228 R279 S281 V282 H283 R308 R311 G312 D323
BS04	DAR	A	S63 G64 V65 Y68 E225 C271 E314	S62 G63 V64 Y67 E224 C270 E313

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

External links

• PDB: RCSB:1bg0, PDBe:1bg0, PDBj:1bg0
• PDBsum: 1bg0
• PubMed: 9671698
• UniProt: P51541|KARG_LIMPO Arginine kinase