4F4J

Conversion of the enzyme guanylate kinase into a mitotic spindle orienting protein by a single mutation that inhibits gmp- induced closing

Replaces:  3SQK

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004385	molecular_function	GMP kinase activity
A	0005524	molecular_function	ATP binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006163	biological_process	purine nucleotide metabolic process
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0046037	biological_process	GMP metabolic process
A	0046711	biological_process	GDP biosynthetic process
B	0000166	molecular_function	nucleotide binding
B	0004385	molecular_function	GMP kinase activity
B	0005524	molecular_function	ATP binding
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006163	biological_process	purine nucleotide metabolic process
B	0016301	molecular_function	kinase activity
B	0016740	molecular_function	transferase activity
B	0046037	biological_process	GMP metabolic process
B	0046711	biological_process	GDP biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 A 201

Chain	Residue
A	SER11
A	GLY12
A	THR13
A	GLY14
A	LYS15
A	SER16
B	ALA43
B	GLY44

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 B 201

Chain	Residue
B	GLY12
B	THR13
B	GLY14
B	LYS15
B	SER16
B	SER11

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B 202

Chain	Residue
A	THR40
A	ARG42
A	ASN77
B	SER11
B	ARG147

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B 203

Chain	Residue
A	GLU142
A	LYS146
B	SER55
B	VAL56
B	HOH331

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B 204

Chain	Residue
B	SER0
B	PHE74
B	SER75
B	ASN115
B	HOH320

---

Functional Information from PROSITE/UniProt

site_id	PS00856
Number of Residues	18
Details	GUANYLATE_KINASE_1 Guanylate kinase-like signature. TTRtpRagEvnGkdYnFV

Chain	Residue	Details
A	THR37-VAL54

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	182
Details	Domain: {"description":"Guanylate kinase-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00100","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	14
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00100","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"PubMed","id":"1314905","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1967656","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1GKY","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Modified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"1314905","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2551688","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17287358","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"17330950","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---