3BP3: EIIB

Crystal structure of EIIB. Determined by X-ray diffraction at 1.65 Å resolution. Released 4 Nov 2008.

Method
X-ray diffraction
Resolution
1.65 Å
Organism
Escherichia coli
Chains
2
Atoms
1,297
Mol. weight
17.36 kDa
Released
4 Nov 2008

Explore 3BP3 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3BP3 contains 12 α-helices and 9 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 6 helices, 4 β-strands

ElementResiduesLengthSheet
α-helix13-208
α-helix24-263
β-strand27-3261
β-strand36-4161
α-helix44-463
α-helix49-546
β-strand59-6351
β-strand66-7051
α-helix72-743
α-helix75-8713
Chain B: 6 helices, 5 β-strands
ElementResiduesLengthSheet
β-strand10-1121
α-helix13-208
α-helix24-263
β-strand27-3262
β-strand36-4162
α-helix44-463
α-helix49-546
β-strand59-6352
β-strand66-7052
α-helix72-743
α-helix75-8713

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Glucose-specific phosphotransferase enzyme IIB componentA, Bprotein82Escherichia coliP69786 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>3BP3_1 Glucose-specific phosphotransferase enzyme IIB component (chains A, B)
TGTSEMAPALVAAFGGKENITNLDACITRLRVSVADVSKVDQAGLKKLGAAGVVVAGSGV
QAIFGTKSDNLKTEMDEYIRNH

Primary citation

Analyses of Mlc-IIBGlc interaction and a plausible molecular mechanism of Mlc inactivation by membrane sequestration. Nam, T.W., Jung, H.I., An, Y.J. et al. Proc Natl Acad Sci U S A (2008) 105:3751-3756. DOI 10.1073/pnas.0709295105 · PubMed

Other PDB entries of the same protein (UniProt P69786 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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