Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4I02

structure of the mutant Catabolite gene activator protein V140A

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003677	molecular_function	DNA binding
A	0003680	molecular_function	minor groove of adenine-thymine-rich DNA binding
A	0003700	molecular_function	DNA-binding transcription factor activity
A	0005515	molecular_function	protein binding
A	0005829	cellular_component	cytosol
A	0006351	biological_process	DNA-templated transcription
A	0006355	biological_process	regulation of DNA-templated transcription
A	0008301	molecular_function	DNA binding, bending
A	0030552	molecular_function	cAMP binding
A	0032993	cellular_component	protein-DNA complex
A	0042802	molecular_function	identical protein binding
A	0043565	molecular_function	sequence-specific DNA binding
A	0045013	biological_process	carbon catabolite repression of transcription
A	0045892	biological_process	negative regulation of DNA-templated transcription
A	0045893	biological_process	positive regulation of DNA-templated transcription
B	0000166	molecular_function	nucleotide binding
B	0003677	molecular_function	DNA binding
B	0003680	molecular_function	minor groove of adenine-thymine-rich DNA binding
B	0003700	molecular_function	DNA-binding transcription factor activity
B	0005515	molecular_function	protein binding
B	0005829	cellular_component	cytosol
B	0006351	biological_process	DNA-templated transcription
B	0006355	biological_process	regulation of DNA-templated transcription
B	0008301	molecular_function	DNA binding, bending
B	0030552	molecular_function	cAMP binding
B	0032993	cellular_component	protein-DNA complex
B	0042802	molecular_function	identical protein binding
B	0043565	molecular_function	sequence-specific DNA binding
B	0045013	biological_process	carbon catabolite repression of transcription
B	0045892	biological_process	negative regulation of DNA-templated transcription
B	0045893	biological_process	positive regulation of DNA-templated transcription
C	0000166	molecular_function	nucleotide binding
C	0003677	molecular_function	DNA binding
C	0003680	molecular_function	minor groove of adenine-thymine-rich DNA binding
C	0003700	molecular_function	DNA-binding transcription factor activity
C	0005515	molecular_function	protein binding
C	0005829	cellular_component	cytosol
C	0006351	biological_process	DNA-templated transcription
C	0006355	biological_process	regulation of DNA-templated transcription
C	0008301	molecular_function	DNA binding, bending
C	0030552	molecular_function	cAMP binding
C	0032993	cellular_component	protein-DNA complex
C	0042802	molecular_function	identical protein binding
C	0043565	molecular_function	sequence-specific DNA binding
C	0045013	biological_process	carbon catabolite repression of transcription
C	0045892	biological_process	negative regulation of DNA-templated transcription
C	0045893	biological_process	positive regulation of DNA-templated transcription
D	0000166	molecular_function	nucleotide binding
D	0003677	molecular_function	DNA binding
D	0003680	molecular_function	minor groove of adenine-thymine-rich DNA binding
D	0003700	molecular_function	DNA-binding transcription factor activity
D	0005515	molecular_function	protein binding
D	0005829	cellular_component	cytosol
D	0006351	biological_process	DNA-templated transcription
D	0006355	biological_process	regulation of DNA-templated transcription
D	0008301	molecular_function	DNA binding, bending
D	0030552	molecular_function	cAMP binding
D	0032993	cellular_component	protein-DNA complex
D	0042802	molecular_function	identical protein binding
D	0043565	molecular_function	sequence-specific DNA binding
D	0045013	biological_process	carbon catabolite repression of transcription
D	0045892	biological_process	negative regulation of DNA-templated transcription
D	0045893	biological_process	positive regulation of DNA-templated transcription
E	0000166	molecular_function	nucleotide binding
E	0003677	molecular_function	DNA binding
E	0003680	molecular_function	minor groove of adenine-thymine-rich DNA binding
E	0003700	molecular_function	DNA-binding transcription factor activity
E	0005515	molecular_function	protein binding
E	0005829	cellular_component	cytosol
E	0006351	biological_process	DNA-templated transcription
E	0006355	biological_process	regulation of DNA-templated transcription
E	0008301	molecular_function	DNA binding, bending
E	0030552	molecular_function	cAMP binding
E	0032993	cellular_component	protein-DNA complex
E	0042802	molecular_function	identical protein binding
E	0043565	molecular_function	sequence-specific DNA binding
E	0045013	biological_process	carbon catabolite repression of transcription
E	0045892	biological_process	negative regulation of DNA-templated transcription
E	0045893	biological_process	positive regulation of DNA-templated transcription
F	0000166	molecular_function	nucleotide binding
F	0003677	molecular_function	DNA binding
F	0003680	molecular_function	minor groove of adenine-thymine-rich DNA binding
F	0003700	molecular_function	DNA-binding transcription factor activity
F	0005515	molecular_function	protein binding
F	0005829	cellular_component	cytosol
F	0006351	biological_process	DNA-templated transcription
F	0006355	biological_process	regulation of DNA-templated transcription
F	0008301	molecular_function	DNA binding, bending
F	0030552	molecular_function	cAMP binding
F	0032993	cellular_component	protein-DNA complex
F	0042802	molecular_function	identical protein binding
F	0043565	molecular_function	sequence-specific DNA binding
F	0045013	biological_process	carbon catabolite repression of transcription
F	0045892	biological_process	negative regulation of DNA-templated transcription
F	0045893	biological_process	positive regulation of DNA-templated transcription

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	BINDING SITE FOR RESIDUE CMP A 301

Chain	Residue
A	ILE31
A	ALA85
A	VAL87
A	ARG124
A	THR128
A	HOH401
A	HOH403
A	HOH410
E	LEU125
E	SER129
A	VAL50
A	SER63
A	ILE71
A	GLY72
A	GLU73
A	LEU74
A	ARG83
A	SER84

site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE CMP A 302

Chain	Residue
A	LYS58
A	GLU59
A	GLN171
A	GLY174
A	GLN175
A	GLY178
A	CYS179
A	SER180
A	ARG181
A	HOH500
E	ALA136

site_id	AC3
Number of Residues	16
Details	BINDING SITE FOR RESIDUE CMP B 301

Chain	Residue
B	ILE31
B	VAL50
B	SER63
B	ILE71
B	GLY72
B	GLU73
B	LEU74
B	ARG83
B	SER84
B	ALA85
B	THR128
B	HOH402
B	HOH419
B	HOH420
C	LEU125
C	SER129

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE CMP B 302

Chain	Residue
B	LYS58
B	GLU59
B	GLN171
B	GLY174
B	GLN175
B	GLY178
B	CYS179
B	SER180
B	ARG181
C	ALA136

site_id	AC5
Number of Residues	21
Details	BINDING SITE FOR RESIDUE CMP C 301

Chain	Residue
B	LEU125
B	SER129
C	ILE31
C	VAL50
C	LEU62
C	SER63
C	ILE71
C	GLY72
C	GLU73
C	LEU74
C	GLY75
C	ARG83
C	SER84
C	ALA85
C	VAL87
C	ARG124
C	THR128
C	HOH402
C	HOH406
C	HOH420
C	HOH527

site_id	AC6
Number of Residues	17
Details	BINDING SITE FOR RESIDUE CMP D 301

Chain	Residue
D	VAL50
D	LEU62
D	SER63
D	ILE71
D	GLY72
D	GLU73
D	LEU74
D	ARG83
D	SER84
D	ALA85
D	VAL87
D	THR128
D	HOH401
D	HOH402
F	LEU125
F	SER129
F	HOH422

site_id	AC7
Number of Residues	13
Details	BINDING SITE FOR RESIDUE CMP D 302

Chain	Residue
D	CYS179
D	SER180
D	ARG181
D	HOH492
D	HOH512
D	HOH547
F	ALA136
D	LYS58
D	GLU59
D	GLN171
D	GLY174
D	GLN175
D	GLY178

site_id	AC8
Number of Residues	20
Details	BINDING SITE FOR RESIDUE CMP E 301

Chain	Residue
A	LEU125
A	SER129
A	HOH432
E	ILE31
E	VAL50
E	LEU62
E	SER63
E	ILE71
E	GLY72
E	GLU73
E	LEU74
E	ARG83
E	SER84
E	ALA85
E	VAL87
E	ARG124
E	THR128
E	HOH403
E	HOH404
E	HOH473

site_id	AC9
Number of Residues	19
Details	BINDING SITE FOR RESIDUE CMP F 301

Chain	Residue
D	LEU125
D	SER129
F	ILE31
F	VAL50
F	LEU62
F	SER63
F	ILE71
F	GLY72
F	GLU73
F	LEU74
F	ARG83
F	SER84
F	ALA85
F	VAL87
F	ARG124
F	THR128
F	HOH403
F	HOH405
F	HOH433

Functional Information from PROSITE/UniProt

site_id	PS00042
Number of Residues	24
Details	HTH_CRP_1 Crp-type HTH domain signature. ITRqeIGqIVGcSreTv.GRiLkmL

Chain	Residue	Details
A	ILE168-LEU191

site_id	PS00888
Number of Residues	17
Details	CNMP_BINDING_1 Cyclic nucleotide-binding domain signature 1. LIhQGEkAEtLYYIvkG

Chain	Residue	Details
A	LEU30-GLY46

site_id	PS00889
Number of Residues	19
Details	CNMP_BINDING_2 Cyclic nucleotide-binding domain signature 2. IGElGLfeegqe.....RSAwVrA

Chain	Residue	Details
A	ILE71-ALA89

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	36
Details	DNA binding: {"description":"H-T-H motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU00387","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	12
Details	Region: {"description":"Activating region 2 (AR2); probably contacts the N-terminus of RpoA","evidences":[{"source":"PubMed","id":"8978616","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	36
Details	Region: {"description":"Activating region 3 (AR3); probably contacts sigma-70 (RpoD)","evidences":[{"source":"PubMed","id":"10860739","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10860740","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	54
Details	Region: {"description":"Activating region 1 (AR1); probably contacts the C-terminus of RpoA","evidences":[{"source":"PubMed","id":"7966284","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8392187","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	126
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11124031","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12202833","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1653449","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2828639","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6286624","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8757802","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	6
Details	Site: {"description":"Activating region 2 (AR2); probably contacts the N-terminus of RpoA","evidences":[{"source":"PubMed","id":"8978616","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	6
Details	Site: {"description":"Activating region 2 (AR2); probably contacts the N-terminus of RpoA","evidences":[{"source":"PubMed","id":"15520470","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8978616","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	6
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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