Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3BP8

Crystal structure of Mlc/EIIB complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0006351biological_processDNA-templated transcription
A0006355biological_processregulation of DNA-templated transcription
A0016020cellular_componentmembrane
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
B0003677molecular_functionDNA binding
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0006351biological_processDNA-templated transcription
B0006355biological_processregulation of DNA-templated transcription
B0016020cellular_componentmembrane
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
C0008982molecular_functionprotein-N(PI)-phosphohistidine-sugar phosphotransferase activity
C0009401biological_processphosphoenolpyruvate-dependent sugar phosphotransferase system
D0008982molecular_functionprotein-N(PI)-phosphohistidine-sugar phosphotransferase activity
D0009401biological_processphosphoenolpyruvate-dependent sugar phosphotransferase system
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT A 408
ChainResidue
ALEU234
AHIS236
BTHR230

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT A 409
ChainResidue
AASP349
BASP251

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 410
ChainResidue
AHIS247
ACYS257
ACYS259
ACYS264

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 407
ChainResidue
BHIS247
BCYS257
BCYS259
BCYS264

Functional Information from PROSITE/UniProt
site_idPS01035
Number of Residues18
DetailsPTS_EIIB_TYPE_1_CYS PTS EIIB domains cysteine phosphorylation site signature. NItnldaCiTRLrVsVaD
ChainResidueDetails
CASN26-ASP43

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues18
DetailsDNA binding: {"description":"H-T-H motif","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15929984","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18319344","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1Z6R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3BP8","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"description":"Phosphocysteine intermediate; for EIIB activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU00421","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12716891","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"18319344","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"3129430","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphocysteine","evidences":[{"source":"PubMed","id":"8505292","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1q18
ChainResidueDetails
AASP195

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1q18
ChainResidueDetails
BASP195

239149

PDB entries from 2025-07-23

PDB statisticsPDBj update infoContact PDBjnumon