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

3GN5

Structure of the E. coli protein MqsA (YgiT/b3021)

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0005515molecular_functionprotein binding
A0006355biological_processregulation of DNA-templated transcription
A0042803molecular_functionprotein homodimerization activity
A0043565molecular_functionsequence-specific DNA binding
A0044010biological_processsingle-species biofilm formation
A0046872molecular_functionmetal ion binding
A0110001cellular_componenttoxin-antitoxin complex
B0003677molecular_functionDNA binding
B0005515molecular_functionprotein binding
B0006355biological_processregulation of DNA-templated transcription
B0042803molecular_functionprotein homodimerization activity
B0043565molecular_functionsequence-specific DNA binding
B0044010biological_processsingle-species biofilm formation
B0046872molecular_functionmetal ion binding
B0110001cellular_componenttoxin-antitoxin complex
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 132
ChainResidue
ACYS3
ACYS6
ACYS37
ACYS40

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 3968
ChainResidue
AARG23
AASN65
ATHR68
AHOH257

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 132
ChainResidue
BCYS6
BCYS37
BCYS40
BCYS3

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues19
DetailsDNA_BIND: H-T-H motif => ECO:0000255|PROSITE-ProRule:PRU00257
ChainResidueDetails
BGLN85-LYS104

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:20041169, ECO:0000269|PubMed:20823526, ECO:0000269|PubMed:21068382, ECO:0000269|PubMed:22789559
ChainResidueDetails
BCYS3
BCYS6
BCYS37
BCYS40

225946

PDB entries from 2024-10-09

PDB statisticsPDBj update infoContact PDBjnumon