8WTB

Crystal structure of McsA/McsB complex truncated by chymotrypsin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003824	molecular_function	catalytic activity
A	0004111	molecular_function	creatine kinase activity
A	0004672	molecular_function	protein kinase activity
A	0005524	molecular_function	ATP binding
A	0005615	cellular_component	extracellular space
A	0005737	cellular_component	cytoplasm
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0016772	molecular_function	transferase activity, transferring phosphorus-containing groups
A	0016775	molecular_function	phosphotransferase activity, nitrogenous group as acceptor
A	0046314	biological_process	phosphocreatine biosynthetic process
B	0005507	molecular_function	copper ion binding
B	0006508	biological_process	proteolysis
B	0008270	molecular_function	zinc ion binding
B	0046870	molecular_function	cadmium ion binding
B	0050897	molecular_function	cobalt ion binding
B	1990169	biological_process	stress response to copper ion
B	1990170	biological_process	stress response to cadmium ion
C	0000166	molecular_function	nucleotide binding
C	0003824	molecular_function	catalytic activity
C	0004111	molecular_function	creatine kinase activity
C	0004672	molecular_function	protein kinase activity
C	0005524	molecular_function	ATP binding
C	0005615	cellular_component	extracellular space
C	0005737	cellular_component	cytoplasm
C	0016301	molecular_function	kinase activity
C	0016740	molecular_function	transferase activity
C	0016772	molecular_function	transferase activity, transferring phosphorus-containing groups
C	0016775	molecular_function	phosphotransferase activity, nitrogenous group as acceptor
C	0046314	biological_process	phosphocreatine biosynthetic process
D	0005507	molecular_function	copper ion binding
D	0006508	biological_process	proteolysis
D	0008270	molecular_function	zinc ion binding
D	0046870	molecular_function	cadmium ion binding
D	0050897	molecular_function	cobalt ion binding
D	1990169	biological_process	stress response to copper ion
D	1990170	biological_process	stress response to cadmium ion

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	CYS167-THR173

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	30
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00602","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	4
Details	Modified residue: {"description":"Phosphoarginine; by autocatalysis","evidences":[{"source":"PubMed","id":"21622759","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Modified residue: {"description":"Phosphoarginine; by autocatalysis","evidences":[{"source":"PubMed","id":"24263382","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	70
Details	Domain: {"description":"UVR","evidences":[{"source":"PROSITE-ProRule","id":"PRU00217","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"Phosphoarginine","evidences":[{"source":"PubMed","id":"24263382","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"Phosphoarginine","evidences":[{"source":"PubMed","id":"22517742","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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