Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2V4Y

THE STRUCTURE OF E. COLI UMP KINASE IN COMPLEX WITH ITS ALLOSTERIC REGULATOR GTP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006221	biological_process	pyrimidine nucleotide biosynthetic process
A	0006225	biological_process	UDP biosynthetic process
A	0009041	molecular_function	UMP/dUMP kinase activity
A	0016301	molecular_function	kinase activity
A	0016310	biological_process	phosphorylation
A	0033862	molecular_function	UMP kinase activity
A	0042802	molecular_function	identical protein binding
A	0044210	biological_process	'de novo' CTP biosynthetic process
A	0046940	biological_process	nucleoside monophosphate phosphorylation
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006221	biological_process	pyrimidine nucleotide biosynthetic process
B	0006225	biological_process	UDP biosynthetic process
B	0009041	molecular_function	UMP/dUMP kinase activity
B	0016301	molecular_function	kinase activity
B	0016310	biological_process	phosphorylation
B	0033862	molecular_function	UMP kinase activity
B	0042802	molecular_function	identical protein binding
B	0044210	biological_process	'de novo' CTP biosynthetic process
B	0046940	biological_process	nucleoside monophosphate phosphorylation
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006221	biological_process	pyrimidine nucleotide biosynthetic process
C	0006225	biological_process	UDP biosynthetic process
C	0009041	molecular_function	UMP/dUMP kinase activity
C	0016301	molecular_function	kinase activity
C	0016310	biological_process	phosphorylation
C	0033862	molecular_function	UMP kinase activity
C	0042802	molecular_function	identical protein binding
C	0044210	biological_process	'de novo' CTP biosynthetic process
C	0046940	biological_process	nucleoside monophosphate phosphorylation
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006221	biological_process	pyrimidine nucleotide biosynthetic process
D	0006225	biological_process	UDP biosynthetic process
D	0009041	molecular_function	UMP/dUMP kinase activity
D	0016301	molecular_function	kinase activity
D	0016310	biological_process	phosphorylation
D	0033862	molecular_function	UMP kinase activity
D	0042802	molecular_function	identical protein binding
D	0044210	biological_process	'de novo' CTP biosynthetic process
D	0046940	biological_process	nucleoside monophosphate phosphorylation
E	0005524	molecular_function	ATP binding
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0006221	biological_process	pyrimidine nucleotide biosynthetic process
E	0006225	biological_process	UDP biosynthetic process
E	0009041	molecular_function	UMP/dUMP kinase activity
E	0016301	molecular_function	kinase activity
E	0016310	biological_process	phosphorylation
E	0033862	molecular_function	UMP kinase activity
E	0042802	molecular_function	identical protein binding
E	0044210	biological_process	'de novo' CTP biosynthetic process
E	0046940	biological_process	nucleoside monophosphate phosphorylation
F	0005524	molecular_function	ATP binding
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0006221	biological_process	pyrimidine nucleotide biosynthetic process
F	0006225	biological_process	UDP biosynthetic process
F	0009041	molecular_function	UMP/dUMP kinase activity
F	0016301	molecular_function	kinase activity
F	0016310	biological_process	phosphorylation
F	0033862	molecular_function	UMP kinase activity
F	0042802	molecular_function	identical protein binding
F	0044210	biological_process	'de novo' CTP biosynthetic process
F	0046940	biological_process	nucleoside monophosphate phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE GTP A 1242

Chain	Residue
A	ARG92
E	SER124
E	ARG127
F	ASN72
F	VAL75
A	ASP93
A	HIS96
A	ASN101
A	ALA102
A	ARG103
A	ARG130
E	TRP119
E	ALA120

site_id	AC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE GTP B 1242

Chain	Residue
A	TRP119
A	ALA120
A	SER124
A	ARG127
B	ARG92
B	ASP93
B	HIS96
B	ASN101
B	ALA102
B	ARG103
B	ARG130
D	ASN72
D	VAL75

site_id	AC3
Number of Residues	14
Details	BINDING SITE FOR RESIDUE GTP C 1242

Chain	Residue
B	LYS6
C	ARG92
C	ASP93
C	HIS96
C	ASN101
C	ALA102
C	ARG103
C	ARG130
E	ASN72
E	VAL75
F	TRP119
F	ALA120
F	SER124
F	ARG127

site_id	AC4
Number of Residues	13
Details	BINDING SITE FOR RESIDUE GTP D 1242

Chain	Residue
B	ASN72
B	VAL75
C	TRP119
C	ALA120
C	SER124
C	ARG127
D	ARG92
D	ASP93
D	HIS96
D	ASN101
D	ALA102
D	ARG103
D	ARG130

site_id	AC5
Number of Residues	14
Details	BINDING SITE FOR RESIDUE GTP E 1242

Chain	Residue
B	TRP119
B	ALA120
B	SER124
B	ARG127
C	ASN72
C	VAL75
E	ARG92
E	ASP93
E	HIS96
E	ASN101
E	ALA102
E	ARG103
E	ARG130
F	LYS6

site_id	AC6
Number of Residues	12
Details	BINDING SITE FOR RESIDUE GTP F 1242

Chain	Residue
A	ASN72
D	TRP119
D	ALA120
D	SER124
D	ARG127
F	ARG92
F	ASP93
F	HIS96
F	ASN101
F	ALA102
F	ARG103
F	ARG130

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GTP F 1243

Chain	Residue
F	SER17
F	GLY18
F	GLU19
F	GLY56
F	GLY57
F	GLY58
F	THR144
F	THR145

site_id	AC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GTP A 1243

Chain	Residue
A	SER17
A	GLY18
A	GLU19
A	GLY56
A	GLY57
A	GLY58
A	THR144
A	THR145

site_id	AC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GTP B 1243

Chain	Residue
B	GLY57
B	GLY58
B	THR144
B	THR145
B	HOH2003
B	SER17
B	GLY18
B	GLU19
B	GLY56

site_id	BC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GTP D 1243

Chain	Residue
D	SER17
D	GLY18
D	GLU19
D	GLY56
D	GLY57
D	GLY58
D	THR144
D	THR145
D	HOH2003

site_id	BC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GTP C 1243

Chain	Residue
C	SER17
C	GLY18
C	GLU19
C	GLY56
C	GLY57
C	GLY58
C	THR144
C	THR145

site_id	BC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GTP E 1243

Chain	Residue
E	SER17
E	GLY18
E	GLU19
E	GLY56
E	GLY57
E	GLY58
E	THR144
E	THR145
E	HOH2002

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	18
Details	BINDING: BINDING => ECO:0000269\|PubMed:15857829, ECO:0000269\|PubMed:18945668, ECO:0007744\|PDB:2BND, ECO:0007744\|PDB:2BNF, ECO:0007744\|PDB:2V4Y

Chain	Residue	Details
A	LYS15
D	LYS15
D	GLY57
D	GLY58
E	LYS15
E	GLY57
E	GLY58
F	LYS15
F	GLY57
F	GLY58
A	GLY57
A	GLY58
B	LYS15
B	GLY57
B	GLY58
C	LYS15
C	GLY57
C	GLY58

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269\|PubMed:15857829, ECO:0007744\|PDB:2BND, ECO:0007744\|PDB:2BNE, ECO:0007744\|PDB:2BNF

Chain	Residue	Details
A	ARG62
B	ARG62
C	ARG62
D	ARG62
E	ARG62
F	ARG62

site_id	SWS_FT_FI3
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269\|PubMed:15857829, ECO:0000269\|PubMed:18945668, ECO:0007744\|PDB:2BNE, ECO:0007744\|PDB:2BNF, ECO:0007744\|PDB:2V4Y

Chain	Residue	Details
A	ASP77
B	ASP77
C	ASP77
D	ASP77
E	ASP77
F	ASP77

site_id	SWS_FT_FI4
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:18945668, ECO:0007744\|PDB:2V4Y

Chain	Residue	Details
A	ARG92
E	ASN101
F	ARG92
F	ASN101
A	ASN101
B	ARG92
B	ASN101
C	ARG92
C	ASN101
D	ARG92
D	ASN101
E	ARG92

site_id	SWS_FT_FI5
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269\|PubMed:15857829, ECO:0000269\|PubMed:18945668, ECO:0007744\|PDB:2BND, ECO:0007744\|PDB:2BNE, ECO:0007744\|PDB:2BNF, ECO:0007744\|PDB:2V4Y

Chain	Residue	Details
A	THR138
B	THR138
C	THR138
D	THR138
E	THR138
F	THR138

site_id	SWS_FT_FI6
Number of Residues	18
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	THR165
D	THR165
D	PHE171
D	ASP174
E	THR165
E	PHE171
E	ASP174
F	THR165
F	PHE171
F	ASP174
A	PHE171
A	ASP174
B	THR165
B	PHE171
B	ASP174
C	THR165
C	PHE171
C	ASP174

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