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3C3W

Crystal Structure of the Mycobacterium tuberculosis Hypoxic Response Regulator DosR

Functional Information from GO Data
ChainGOidnamespacecontents
A0000160biological_processphosphorelay signal transduction system
A0001666biological_processresponse to hypoxia
A0003677molecular_functionDNA binding
A0003700molecular_functionDNA-binding transcription factor activity
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006355biological_processregulation of DNA-templated transcription
A0009274cellular_componentpeptidoglycan-based cell wall
A0022611biological_processdormancy process
A0044161cellular_componenthost cell cytoplasmic vesicle
A0045893biological_processpositive regulation of DNA-templated transcription
A0072493cellular_componenthost cell endosome lumen
B0000160biological_processphosphorelay signal transduction system
B0001666biological_processresponse to hypoxia
B0003677molecular_functionDNA binding
B0003700molecular_functionDNA-binding transcription factor activity
B0005615cellular_componentextracellular space
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006355biological_processregulation of DNA-templated transcription
B0009274cellular_componentpeptidoglycan-based cell wall
B0022611biological_processdormancy process
B0044161cellular_componenthost cell cytoplasmic vesicle
B0045893biological_processpositive regulation of DNA-templated transcription
B0072493cellular_componenthost cell endosome lumen
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 226
ChainResidue
AARG67
AARG113
AASP117
BARG67
BARG113
BASP117

Functional Information from PROSITE/UniProt
site_idPS00622
Number of Residues28
DetailsHTH_LUXR_1 LuxR-type HTH domain signature. GltNkqIAdrMfLaekTVknYvsRLlaK
ChainResidueDetails
AGLY164-LYS191

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues38
DetailsDNA_BIND: H-T-H motif => ECO:0000255|PROSITE-ProRule:PRU00411
ChainResidueDetails
AASN167-SER186
BASN167-SER186

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: 4-aspartylphosphate => ECO:0000255|PROSITE-ProRule:PRU00169, ECO:0000305|PubMed:15033981, ECO:0000305|PubMed:15073296
ChainResidueDetails
AASP54
BASP54

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphothreonine; by PknH => ECO:0000269|PubMed:20630871
ChainResidueDetails
ATHR198
ATHR205
BTHR198
BTHR205

227111

PDB entries from 2024-11-06

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