5U92

Crystal Structure of arginine kinase from the spider Polybetes pythagoricus in complex with arginine

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003824	molecular_function	catalytic activity
A	0004054	molecular_function	arginine kinase activity
A	0004111	molecular_function	creatine kinase activity
A	0005524	molecular_function	ATP binding
A	0005615	cellular_component	extracellular space
A	0016301	molecular_function	kinase activity
A	0016310	biological_process	phosphorylation
A	0016740	molecular_function	transferase activity
A	0016772	molecular_function	transferase activity, transferring phosphorus-containing groups
A	0046314	biological_process	phosphocreatine biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	binding site for residue ARG A 401

Chain	Residue
A	SER63
A	GLY64
A	VAL65
A	GLY66
A	TYR68
A	GLU225
A	CYS271
A	HOH557
A	HOH566

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site_id	AC2
Number of Residues	2
Details	binding site for residue NA A 402

Chain	Residue
A	TYR89
A	LYS328

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site_id	AC3
Number of Residues	2
Details	binding site for residue NA A 403

Chain	Residue
A	ASP344
A	GLU348

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Functional Information from PROSITE/UniProt

site_id	PS00112
Number of Residues	7
Details	PHOSPHAGEN_KINASE Phosphagen kinase active site signature. CP.TNLGT

Chain	Residue	Details
A	CYS271-THR277

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"28924503","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5U92","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00843","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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