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4I0A

structure of the mutant Catabolite gene activator protein V132A

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 Residues16
DetailsBINDING SITE FOR RESIDUE CMP A 301
ChainResidue
AVAL50
AVAL87
AARG124
ATHR128
AHOH401
AHOH404
BSER129
BHOH414
ASER63
AILE71
AGLY72
AGLU73
ALEU74
AARG83
ASER84
AALA85

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE CMP A 302
ChainResidue
ALYS58
AGLU59
AGLN171
AGLY174
AGLN175
AGLY178
ACYS179
ASER180
AARG181
BALA136
BPHE137

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 303
ChainResidue
ALYS131
AASN134
ALEU135
AARG143
AGLN146
ATHR147
AILE176

site_idAC4
Number of Residues17
DetailsBINDING SITE FOR RESIDUE CMP B 301
ChainResidue
ALEU125
ASER129
BVAL50
BSER63
BILE71
BGLY72
BGLU73
BLEU74
BARG83
BSER84
BALA85
BVAL87
BARG124
BTHR128
BHOH409
BHOH410
BHOH417

Functional Information from PROSITE/UniProt
site_idPS00042
Number of Residues24
DetailsHTH_CRP_1 Crp-type HTH domain signature. ITRqeIGqIVGcSreTv.GRiLkmL
ChainResidueDetails
AILE168-LEU191

site_idPS00888
Number of Residues17
DetailsCNMP_BINDING_1 Cyclic nucleotide-binding domain signature 1. LIhQGEkAEtLYYIvkG
ChainResidueDetails
ALEU30-GLY46

site_idPS00889
Number of Residues19
DetailsCNMP_BINDING_2 Cyclic nucleotide-binding domain signature 2. IGElGLfeegqe.....RSAwVrA
ChainResidueDetails
AILE71-ALA89

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsDNA_BIND: H-T-H motif => ECO:0000255|PROSITE-ProRule:PRU00387
ChainResidueDetails
ASER180-ARG186
BSER180-ARG186

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
AGLY57
BTHR128
BALA136
BGLN171
AGLY72
AARG83
ATHR128
AALA136
AGLN171
BGLY57
BGLY72
BARG83

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Activating region 2 (AR2); probably contacts the N-terminus of RpoA => ECO:0000269|PubMed:8978616
ChainResidueDetails
AGLU97
BGLU97

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
ALYS102
BLYS102

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
ALYS101
BLYS101

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PDB entries from 2024-07-24

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