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4FT8

E. coli Catabolite Activator Protein with Cobalt and Sulfate Ligands

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 Residues15
DetailsBINDING SITE FOR RESIDUE CMP A 301
ChainResidue
AVAL49
ATHR127
AHOH415
AHOH417
AHOH475
BLEU124
BSER128
ALEU61
AILE70
AGLY71
AGLU72
ALEU73
AARG82
ASER83
AALA84

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 302
ChainResidue
AHIS21
ALYS22
AHOH570
BLYS35
BGLY79

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 303
ChainResidue
AHIS31
ATRP85
AHOH508
AHOH549
BHIS31
BTRP85
BHOH568

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 304
ChainResidue
AGLY33
AGLU81
AHOH442
AHOH470
AHOH558
BSER27
BTHR28

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 305
ChainResidue
ATHR168
AARG169
AGLN170

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 306
ChainResidue
ATHR90
AALA91
AHOH599
AHOH601

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 307
ChainResidue
AHIS19
AILE20
AHOH482
AHOH566

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO A 308
ChainResidue
AHIS19
AHIS21
AGLU96
AHOH402
BGLU37

site_idAC9
Number of Residues18
DetailsBINDING SITE FOR RESIDUE CMP B 301
ChainResidue
ALEU124
ASER128
BVAL49
BLEU61
BSER62
BILE70
BGLY71
BGLU72
BLEU73
BARG82
BSER83
BALA84
BVAL86
BARG123
BTHR127
BHOH412
BHOH416
BHOH417

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 302
ChainResidue
ALYS35
AHOH478
AHOH583
BILE20
BHIS21
BLYS22
BHOH573

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 303
ChainResidue
BASP68
BGLN119
BARG122
BARG123
BHOH457
BHOH460

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 304
ChainResidue
BASP138
BVAL139
BARG142

site_idBC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 305
ChainResidue
BSER179
BARG180
BHOH590

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 306
ChainResidue
BLYS57
BCYS178
BSER179
BTHR182

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 307
ChainResidue
BTHR168
BARG169
BGLN170
BARG180
BHOH520

site_idBC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 308
ChainResidue
BGLY200
BLYS201
BHOH586
ASER197
ATYR206
BHIS199

site_idBC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO B 309
ChainResidue
AGLU37
AHOH412
BHIS19
BHIS21
BGLU96

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

227344

PDB entries from 2024-11-13

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