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	0000166	molecular_function	nucleotide binding
A	0003824	molecular_function	catalytic activity
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	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
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	0000166	molecular_function	nucleotide binding
B	0003824	molecular_function	catalytic activity
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	0016301	molecular_function	kinase activity
B	0016740	molecular_function	transferase activity
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	0000166	molecular_function	nucleotide binding
C	0003824	molecular_function	catalytic activity
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	0016301	molecular_function	kinase activity
C	0016740	molecular_function	transferase activity
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	0000166	molecular_function	nucleotide binding
D	0003824	molecular_function	catalytic activity
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	0016301	molecular_function	kinase activity
D	0016740	molecular_function	transferase activity
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	0000166	molecular_function	nucleotide binding
E	0003824	molecular_function	catalytic activity
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	0016301	molecular_function	kinase activity
E	0016740	molecular_function	transferase activity
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	0000166	molecular_function	nucleotide binding
F	0003824	molecular_function	catalytic activity
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	0016301	molecular_function	kinase activity
F	0016740	molecular_function	transferase activity
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	30
Details	Region: {"description":"Involved in allosteric activation by GTP","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	30
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15857829","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18945668","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2BND","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BNF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2V4Y","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15857829","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2BND","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BNE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BNF","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15857829","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18945668","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2BNE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BNF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2V4Y","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	36
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18945668","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2V4Y","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	42
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15857829","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18945668","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2BND","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BNE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BNF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2V4Y","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	15
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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