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

3DNV

MDT Protein

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
B0000976molecular_functiontranscription cis-regulatory region binding
B0001046molecular_functioncore promoter sequence-specific DNA binding
B0001217molecular_functionDNA-binding transcription repressor activity
B0003677molecular_functionDNA binding
B0005515molecular_functionprotein binding
B0006351biological_processDNA-templated transcription
B0006355biological_processregulation of DNA-templated transcription
B0032993cellular_componentprotein-DNA complex
B0040008biological_processregulation of growth
B0042803molecular_functionprotein homodimerization activity
B0043565molecular_functionsequence-specific DNA binding
B0045892biological_processnegative regulation of DNA-templated transcription
B0110001cellular_componenttoxin-antitoxin complex
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 834
ChainResidue
ALYS351
ATHR364
AALA365

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 833
ChainResidue
AALA358
ASER359
ALYS363
AARG372
AHIS373

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 836
ChainResidue
APHE318
AARG326
APRO329
AASN216

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 837
ChainResidue
AARG162
AASN165

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 838
ChainResidue
ALYS27
AARG49

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE SO4 A 839
ChainResidue
AARG49

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 840
ChainResidue
BLYS38
BGLN39
BHOH414

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues26
DetailsDNA_BIND: H-T-H motif => ECO:0000255|PROSITE-ProRule:PRU00257, ECO:0000269|PubMed:19150849
ChainResidueDetails
BARG21-ASN47

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:17041039
ChainResidueDetails
AGLN309

site_idSWS_FT_FI3
Number of Residues4
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

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:22999936, ECO:0007744|PDB:3DNT, ECO:0007744|PDB:3HZI, ECO:0007744|PDB:3TPT
ChainResidueDetails
ALYS181

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:17041039, ECO:0000269|PubMed:22999936
ChainResidueDetails
ASER150

223166

PDB entries from 2024-07-31

PDB statisticsPDBj update infoContact PDBjnumon