Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3DNT

structures of MDT proteins

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0000976molecular_functiontranscription cis-regulatory region binding
A0001217molecular_functionDNA-binding transcription repressor activity
A0003677molecular_functionDNA binding
A0004674molecular_functionprotein serine/threonine kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0006355biological_processregulation of DNA-templated transcription
A0022611biological_processdormancy process
A0032993cellular_componentprotein-DNA complex
A0040008biological_processregulation of growth
A0043565molecular_functionsequence-specific DNA binding
A0044010biological_processsingle-species biofilm formation
A0045892biological_processnegative regulation of DNA-templated transcription
A0046677biological_processresponse to antibiotic
A0106310molecular_functionprotein serine kinase activity
A0110001cellular_componenttoxin-antitoxin complex
B0000287molecular_functionmagnesium ion binding
B0000976molecular_functiontranscription cis-regulatory region binding
B0001217molecular_functionDNA-binding transcription repressor activity
B0003677molecular_functionDNA binding
B0004674molecular_functionprotein serine/threonine kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005829cellular_componentcytosol
B0006355biological_processregulation of DNA-templated transcription
B0022611biological_processdormancy process
B0032993cellular_componentprotein-DNA complex
B0040008biological_processregulation of growth
B0043565molecular_functionsequence-specific DNA binding
B0044010biological_processsingle-species biofilm formation
B0045892biological_processnegative regulation of DNA-templated transcription
B0046677biological_processresponse to antibiotic
B0106310molecular_functionprotein serine kinase activity
B0110001cellular_componenttoxin-antitoxin complex
Functional Information from PDB Data
site_idAC1
Number of Residues27
DetailsBINDING SITE FOR RESIDUE ATP A 500
ChainResidue
AVAL98
AVAL233
AGLU234
AARG235
APHE236
AASP237
AGLN252
AHIS311
ALYS313
AASN314
ATYR331
AALA152
AASP332
AMG441
AMG442
AHOH860
AHOH861
AHOH867
AHOH932
AHOH1063
AGLY153
AALA154
AGLN155
ALYS157
AILE179
ALYS181
APRO218

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 441
ChainResidue
AASN314
AASP332
AATP500
AHOH860

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 442
ChainResidue
AGLN309
AASP332
AATP500

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 833
ChainResidue
AALA358
ASER359
ALYS363
AARG372
AHIS373
AHOH1014
AHOH1201

site_idAC5
Number of Residues29
DetailsBINDING SITE FOR RESIDUE ATP B 501
ChainResidue
BASP67
BVAL98
BALA152
BGLY153
BALA154
BGLN155
BLYS157
BILE179
BLYS181
BVAL233
BGLU234
BARG235
BPHE236
BASP237
BGLN252
BHIS311
BLYS313
BASN314
BTYR331
BASP332
BMG441
BMG442
BHOH835
BHOH837
BHOH842
BHOH858
BHOH861
BHOH1011
BHOH1145

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG B 441
ChainResidue
BASP332
BATP501
BHOH1058
BHOH1165

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG B 442
ChainResidue
BASN314
BASP332
BATP501
BHOH835

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 834
ChainResidue
BALA358
BSER359
BLYS363
BARG372
BHIS373

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsDNA_BIND: DNA_BIND => ECO:0000269|PubMed:19150849
ChainResidueDetails
ALYS379-ARG382
BLYS379-ARG382

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:17041039
ChainResidueDetails
AGLN309
BGLN309

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:22999936, ECO:0007744|PDB:3DNT, ECO:0007744|PDB:3FBR, ECO:0007744|PDB:3HZI, ECO:0007744|PDB:3TPT
ChainResidueDetails
AALA152
AGLU234
AHIS311
ATYR331
BALA152
BGLU234
BHIS311
BTYR331

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:22999936, ECO:0007744|PDB:3DNT, ECO:0007744|PDB:3HZI, ECO:0007744|PDB:3TPT
ChainResidueDetails
ALYS181
BLYS181

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:17041039, ECO:0000269|PubMed:22999936
ChainResidueDetails
ASER150
BSER150

223166

PDB entries from 2024-07-31

PDB statisticsPDBj update infoContact PDBjnumon