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1O3Q

PROTEIN-DNA RECOGNITION AND DNA DEFORMATION REVEALED IN CRYSTAL STRUCTURES OF CAP-DNA COMPLEXES

Replaces:  1DB7
Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
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
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE CMP A 1
ChainResidue
AVAL49
ATHR127
ASER128
AILE70
AGLY71
AGLU72
ALEU73
AARG82
ASER83
AALA84
ALEU124

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE CMP A 2
ChainResidue
ALYS57
AGLU58
AMET59
AALA135
AGLN170
AGLY173
AGLN174
ACYS178
AARG180
CDA9

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 Residues6
DetailsDNA_BIND: H-T-H motif => ECO:0000255|PROSITE-ProRule:PRU00387
ChainResidueDetails
ASER179-ARG185

site_idSWS_FT_FI2
Number of Residues6
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
AARG82
ATHR127
AALA135
AGLN170
AGLY56
AGLY71

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Activating region 2 (AR2); probably contacts the N-terminus of RpoA => ECO:0000269|PubMed:8978616
ChainResidueDetails
AGLU96

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Activating region 2 (AR2); probably contacts the N-terminus of RpoA => ECO:0000269|PubMed:15520470, ECO:0000269|PubMed:8978616
ChainResidueDetails
ALYS101

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
ALYS100

218500

PDB entries from 2024-04-17

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