Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2GZW

Crystal structure of the E.coli CRP-cAMP complex

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE CMP A 1301

Chain	Residue
A	VAL49
A	ALA84
A	THR127
A	HOH1303
A	HOH1317
B	SER128
A	LEU61
A	SER62
A	ILE70
A	GLY71
A	GLU72
A	LEU73
A	ARG82
A	SER83

site_id	AC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE CMP A 1302

Chain	Residue
A	LYS57
A	GLU58
A	GLN170
A	GLY173
A	GLN174
A	GLY177
A	CYS178
A	SER179
A	ARG180
A	HOH1355
A	HOH1357
B	ALA135

site_id	AC3
Number of Residues	17
Details	BINDING SITE FOR RESIDUE CMP B 401

Chain	Residue
A	LEU124
A	SER128
A	HOH1322
B	VAL49
B	ILE70
B	GLY71
B	GLU72
B	LEU73
B	GLY74
B	ARG82
B	SER83
B	ALA84
B	VAL86
B	ARG123
B	THR127
B	HOH975
B	HOH977

site_id	AC4
Number of Residues	15
Details	BINDING SITE FOR RESIDUE CMP C 2301

Chain	Residue
C	VAL49
C	LEU61
C	GLY71
C	GLU72
C	LEU73
C	ARG82
C	SER83
C	ALA84
C	VAL86
C	ARG123
C	THR127
C	HOH2303
C	HOH2304
D	SER128
D	HOH3003

site_id	AC5
Number of Residues	12
Details	BINDING SITE FOR RESIDUE CMP C 2302

Chain	Residue
C	LYS57
C	GLU58
C	GLN170
C	GLY173
C	GLN174
C	GLY177
C	CYS178
C	SER179
C	ARG180
C	HOH2363
D	ALA135
D	HOH3067

site_id	AC6
Number of Residues	18
Details	BINDING SITE FOR RESIDUE CMP D 2401

Chain	Residue
C	LEU124
C	SER128
D	ILE30
D	VAL49
D	LEU61
D	ILE70
D	GLY71
D	GLU72
D	LEU73
D	GLY74
D	ARG82
D	SER83
D	ALA84
D	ARG123
D	THR127
D	HOH2974
D	HOH2977
D	HOH2997

site_id	AC7
Number of Residues	12
Details	BINDING SITE FOR RESIDUE CMP B 973

Chain	Residue
B	HOH1037
A	ALA135
A	PHE136
B	LYS57
B	GLU58
B	GLN170
B	GLY173
B	GLN174
B	GLY177
B	CYS178
B	SER179
B	ARG180

site_id	AC8
Number of Residues	11
Details	BINDING SITE FOR RESIDUE CMP D 2973

Chain	Residue
C	ALA135
D	LYS57
D	GLU58
D	GLN170
D	GLY173
D	GLN174
D	GLY177
D	CYS178
D	SER179
D	ARG180
D	HOH3065

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	ILE167-LEU190

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

Chain	Residue	Details
A	LEU29-GLY45

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

Chain	Residue	Details
A	ILE70-ALA88

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
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	8
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	24
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	36
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	84
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	4
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	4
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	4
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)