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

5IUJ

Crystal structure of the DesK-DesR complex in the phosphotransfer state with low Mg2+ (20 mM)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000155molecular_functionphosphorelay sensor kinase activity
A0000160biological_processphosphorelay signal transduction system
A0016020cellular_componentmembrane
A0046983molecular_functionprotein dimerization activity
B0000155molecular_functionphosphorelay sensor kinase activity
B0000160biological_processphosphorelay signal transduction system
B0016020cellular_componentmembrane
B0046983molecular_functionprotein dimerization activity
C0000160biological_processphosphorelay signal transduction system
D0000155molecular_functionphosphorelay sensor kinase activity
D0000160biological_processphosphorelay signal transduction system
D0016020cellular_componentmembrane
D0046983molecular_functionprotein dimerization activity
E0000155molecular_functionphosphorelay sensor kinase activity
E0000160biological_processphosphorelay signal transduction system
E0016020cellular_componentmembrane
E0046983molecular_functionprotein dimerization activity
F0000160biological_processphosphorelay signal transduction system
Functional Information from PDB Data
site_idAC1
Number of Residues15
Detailsbinding site for residue ACP A 401
ChainResidue
AGLU289
AHIS335
AGLY336
ALEU337
ATHR359
AMG402
AHOH501
AASN293
AHIS297
ASER298
AASP320
ATHR323
APHE324
ALYS325
AGLY326

site_idAC2
Number of Residues4
Detailsbinding site for residue MG A 402
ChainResidue
AGLU289
AASN293
AACP401
AHOH501

site_idAC3
Number of Residues17
Detailsbinding site for residue ACP B 401
ChainResidue
BGLU289
BASN293
BLYS296
BHIS297
BSER298
BASP320
BTHR323
BPHE324
BLYS325
BGLY326
BSER330
BHIS335
BGLY336
BLEU337
BTHR359
BMG402
DLYS312

site_idAC4
Number of Residues4
Detailsbinding site for residue MG B 402
ChainResidue
BGLU289
BASN293
BACP401
BHOH501

site_idAC5
Number of Residues3
Detailsbinding site for residue K C 201
ChainResidue
CASN22
CGLU24
CMET27

site_idAC6
Number of Residues15
Detailsbinding site for residue ACP D 401
ChainResidue
DGLU289
DASN293
DHIS297
DSER298
DASP320
DTHR323
DPHE324
DLYS325
DGLY326
DHIS335
DGLY336
DLEU337
DTHR359
DMG402
DHOH501

site_idAC7
Number of Residues4
Detailsbinding site for residue MG D 402
ChainResidue
DGLU289
DASN293
DACP401
DHOH501

site_idAC8
Number of Residues17
Detailsbinding site for residue ACP E 401
ChainResidue
ALYS312
EGLU289
EASN293
EHIS297
ESER298
EASP320
ETHR323
EPHE324
ELYS325
EGLY326
ESER330
EHIS335
EGLY336
ELEU337
ETHR359
EMG402
EHOH501

site_idAC9
Number of Residues4
Detailsbinding site for residue MG E 402
ChainResidue
EGLU289
EASN293
EACP401
EHOH501

site_idAD1
Number of Residues3
Detailsbinding site for residue K F 201
ChainResidue
FASN22
FGLU24
FMET27

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: 4-aspartylphosphate => ECO:0000255|PROSITE-ProRule:PRU00169
ChainResidueDetails
CASP54
FASP54
DGLU188
EGLU188

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon