Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1QK1

CRYSTAL STRUCTURE OF HUMAN UBIQUITOUS MITOCHONDRIAL CREATINE KINASE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004111	molecular_function	creatine kinase activity
A	0005515	molecular_function	protein binding
A	0005739	cellular_component	mitochondrion
A	0005743	cellular_component	mitochondrial inner membrane
A	0016301	molecular_function	kinase 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	0003824	molecular_function	catalytic activity
B	0004111	molecular_function	creatine kinase activity
B	0005515	molecular_function	protein binding
B	0005739	cellular_component	mitochondrion
B	0005743	cellular_component	mitochondrial inner membrane
B	0016301	molecular_function	kinase activity
B	0016772	molecular_function	transferase activity, transferring phosphorus-containing groups
B	0016775	molecular_function	phosphotransferase activity, nitrogenous group as acceptor
B	0046314	biological_process	phosphocreatine biosynthetic process
C	0003824	molecular_function	catalytic activity
C	0004111	molecular_function	creatine kinase activity
C	0005515	molecular_function	protein binding
C	0005739	cellular_component	mitochondrion
C	0005743	cellular_component	mitochondrial inner membrane
C	0016301	molecular_function	kinase 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	0003824	molecular_function	catalytic activity
D	0004111	molecular_function	creatine kinase activity
D	0005515	molecular_function	protein binding
D	0005739	cellular_component	mitochondrion
D	0005743	cellular_component	mitochondrial inner membrane
D	0016301	molecular_function	kinase activity
D	0016772	molecular_function	transferase activity, transferring phosphorus-containing groups
D	0016775	molecular_function	phosphotransferase activity, nitrogenous group as acceptor
D	0046314	biological_process	phosphocreatine biosynthetic process
E	0003824	molecular_function	catalytic activity
E	0004111	molecular_function	creatine kinase activity
E	0005515	molecular_function	protein binding
E	0005739	cellular_component	mitochondrion
E	0005743	cellular_component	mitochondrial inner membrane
E	0016301	molecular_function	kinase activity
E	0016772	molecular_function	transferase activity, transferring phosphorus-containing groups
E	0016775	molecular_function	phosphotransferase activity, nitrogenous group as acceptor
E	0046314	biological_process	phosphocreatine biosynthetic process
F	0003824	molecular_function	catalytic activity
F	0004111	molecular_function	creatine kinase activity
F	0005515	molecular_function	protein binding
F	0005739	cellular_component	mitochondrion
F	0005743	cellular_component	mitochondrial inner membrane
F	0016301	molecular_function	kinase activity
F	0016772	molecular_function	transferase activity, transferring phosphorus-containing groups
F	0016775	molecular_function	phosphotransferase activity, nitrogenous group as acceptor
F	0046314	biological_process	phosphocreatine biosynthetic process
G	0003824	molecular_function	catalytic activity
G	0004111	molecular_function	creatine kinase activity
G	0005515	molecular_function	protein binding
G	0005739	cellular_component	mitochondrion
G	0005743	cellular_component	mitochondrial inner membrane
G	0016301	molecular_function	kinase activity
G	0016772	molecular_function	transferase activity, transferring phosphorus-containing groups
G	0016775	molecular_function	phosphotransferase activity, nitrogenous group as acceptor
G	0046314	biological_process	phosphocreatine biosynthetic process
H	0003824	molecular_function	catalytic activity
H	0004111	molecular_function	creatine kinase activity
H	0005515	molecular_function	protein binding
H	0005739	cellular_component	mitochondrion
H	0005743	cellular_component	mitochondrial inner membrane
H	0016301	molecular_function	kinase activity
H	0016772	molecular_function	transferase activity, transferring phosphorus-containing groups
H	0016775	molecular_function	phosphotransferase activity, nitrogenous group as acceptor
H	0046314	biological_process	phosphocreatine biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 A 400

Chain	Residue
A	ARG125
A	ARG127
A	ARG287

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 B 400

Chain	Residue
B	ARG125
B	ARG127
B	ARG287

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 C 400

Chain	Residue
C	ARG125
C	ARG127
C	ARG287

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 D 400

Chain	Residue
D	ARG125
D	ARG127
D	ARG287

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 E 400

Chain	Residue
E	ARG125
E	ARG127
E	ARG287

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 F 400

Chain	Residue
F	ARG125
F	ARG127
F	ARG287

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 G 400

Chain	Residue
G	ARG125
G	ARG127
G	ARG287
G	ARG315

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 H 400

Chain	Residue
H	ARG125
H	ARG127
H	ARG287

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	CYS278-THR284

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	688
Details	Domain: {"description":"Phosphagen kinase N-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU00842","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	1936
Details	Domain: {"description":"Phosphagen kinase C-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU00843","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	192
Details	Region: {"description":"Cardiolipin-binding","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	104
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00843","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	16
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P25809","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	8
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P00564","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	8
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P30275","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	8
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P07310","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	5
Details	Annotated By Reference To The Literature 1bg0

Chain	Residue	Details
A	ARG231
A	ARG287
A	ARG315
A	ARG127
A	GLU227

site_id	CSA2
Number of Residues	5
Details	Annotated By Reference To The Literature 1bg0

Chain	Residue	Details
B	ARG231
B	ARG287
B	ARG315
B	ARG127
B	GLU227

site_id	CSA3
Number of Residues	5
Details	Annotated By Reference To The Literature 1bg0

Chain	Residue	Details
C	ARG231
C	ARG287
C	ARG315
C	ARG127
C	GLU227

site_id	CSA4
Number of Residues	5
Details	Annotated By Reference To The Literature 1bg0

Chain	Residue	Details
D	ARG231
D	ARG287
D	ARG315
D	ARG127
D	GLU227

site_id	CSA5
Number of Residues	5
Details	Annotated By Reference To The Literature 1bg0

Chain	Residue	Details
E	ARG231
E	ARG287
E	ARG315
E	ARG127
E	GLU227

site_id	CSA6
Number of Residues	5
Details	Annotated By Reference To The Literature 1bg0

Chain	Residue	Details
F	ARG231
F	ARG287
F	ARG315
F	ARG127
F	GLU227

site_id	CSA7
Number of Residues	5
Details	Annotated By Reference To The Literature 1bg0

Chain	Residue	Details
G	ARG231
G	ARG287
G	ARG315
G	ARG127
G	GLU227

site_id	CSA8
Number of Residues	5
Details	Annotated By Reference To The Literature 1bg0

Chain	Residue	Details
H	ARG231
H	ARG287
H	ARG315
H	ARG127
H	GLU227

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)