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1CGP

CATABOLITE GENE ACTIVATOR PROTEIN (CAP)/DNA COMPLEX + ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0003680molecular_functionminor groove of adenine-thymine-rich DNA binding
A0003700molecular_functionDNA-binding transcription factor activity
A0005515molecular_functionprotein binding
A0005829cellular_componentcytosol
A0006351biological_processDNA-templated transcription
A0006355biological_processregulation of DNA-templated transcription
A0008301molecular_functionDNA binding, bending
A0030552molecular_functioncAMP binding
A0032993cellular_componentprotein-DNA complex
A0042802molecular_functionidentical protein binding
A0043565molecular_functionsequence-specific DNA binding
A0045013biological_processcarbon catabolite repression of transcription
A0045892biological_processnegative regulation of DNA-templated transcription
A0045893biological_processpositive regulation of DNA-templated transcription
B0003677molecular_functionDNA binding
B0003680molecular_functionminor groove of adenine-thymine-rich DNA binding
B0003700molecular_functionDNA-binding transcription factor activity
B0005515molecular_functionprotein binding
B0005829cellular_componentcytosol
B0006351biological_processDNA-templated transcription
B0006355biological_processregulation of DNA-templated transcription
B0008301molecular_functionDNA binding, bending
B0030552molecular_functioncAMP binding
B0032993cellular_componentprotein-DNA complex
B0042802molecular_functionidentical protein binding
B0043565molecular_functionsequence-specific DNA binding
B0045013biological_processcarbon catabolite repression of transcription
B0045892biological_processnegative regulation of DNA-templated transcription
B0045893biological_processpositive regulation of DNA-templated transcription
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE CMP A 206
ChainResidue
AVAL49
ASER62
AGLY71
AGLU72
ALEU73
AARG82
ASER83
AALA84
AVAL86
ATHR127
BLEU124
BSER128

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE CMP B 206
ChainResidue
ASER128
BVAL49
BLEU61
BSER62
BILE70
BGLY71
BGLU72
BLEU73
BARG82
BSER83
BALA84
BARG123
BTHR127

site_idS1A
Number of Residues20
Details
ChainResidue
AILE30
AARG82
ASER83
AALA84
ATRP85
AVAL86
AARG123
ALEU124
AGLN125
AVAL126
ATHR127
AVAL49
BSER128
ALEU61
ASER62
ATYR63
ALEU64
AGLY71
AGLU72
ALEU73

site_idS1B
Number of Residues20
Details
ChainResidue
BILE30
BVAL49
BLEU61
BSER62
BTYR63
BLEU64
BGLY71
BGLU72
BLEU73
BARG82
BSER83
BALA84
BTRP85
BVAL86
BARG123
BLEU124
BGLN125
BVAL126
BTHR127
ASER128

Functional Information from PROSITE/UniProt
site_idPS00042
Number of Residues24
DetailsHTH_CRP_1 Crp-type HTH domain signature. ITRqeIGqIVGcSreTv.GRiLkmL
ChainResidueDetails
AILE167-LEU190

site_idPS00888
Number of Residues17
DetailsCNMP_BINDING_1 Cyclic nucleotide-binding domain signature 1. LIhQGEkAEtLYYIvkG
ChainResidueDetails
ALEU29-GLY45

site_idPS00889
Number of Residues19
DetailsCNMP_BINDING_2 Cyclic nucleotide-binding domain signature 2. IGElGLfeegqe.....RSAwVrA
ChainResidueDetails
AILE70-ALA88

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsDNA_BIND: H-T-H motif => ECO:0000255|PROSITE-ProRule:PRU00387
ChainResidueDetails
ASER179-ARG185
BSER179-ARG185

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:11124031, ECO:0000269|PubMed:12202833, ECO:0000269|PubMed:1653449, ECO:0000269|PubMed:2828639, ECO:0000269|PubMed:6286624, ECO:0000269|PubMed:8757802
ChainResidueDetails
AGLY56
BTHR127
BALA135
BGLN170
AGLY71
AARG82
ATHR127
AALA135
AGLN170
BGLY56
BGLY71
BARG82

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Activating region 2 (AR2); probably contacts the N-terminus of RpoA => ECO:0000269|PubMed:8978616
ChainResidueDetails
AGLU96
BGLU96

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Activating region 2 (AR2); probably contacts the N-terminus of RpoA => ECO:0000269|PubMed:15520470, ECO:0000269|PubMed:8978616
ChainResidueDetails
ALYS101
BLYS101

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
ALYS100
BLYS100

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PDB entries from 2024-05-01

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