Crystal structure of EIIB. Determined by X-ray diffraction at 1.65 Å resolution. Released 4 Nov 2008.
Explore 3BP3 in 3D Show helices and sheets RCSB PDB PDBe
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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 13-20 | 8 | |
| α-helix | 24-26 | 3 | |
| β-strand | 27-32 | 6 | 1 |
| β-strand | 36-41 | 6 | 1 |
| α-helix | 44-46 | 3 | |
| α-helix | 49-54 | 6 | |
| β-strand | 59-63 | 5 | 1 |
| β-strand | 66-70 | 5 | 1 |
| α-helix | 72-74 | 3 | |
| α-helix | 75-87 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 10-11 | 2 | 1 |
| α-helix | 13-20 | 8 | |
| α-helix | 24-26 | 3 | |
| β-strand | 27-32 | 6 | 2 |
| β-strand | 36-41 | 6 | 2 |
| α-helix | 44-46 | 3 | |
| α-helix | 49-54 | 6 | |
| β-strand | 59-63 | 5 | 2 |
| β-strand | 66-70 | 5 | 2 |
| α-helix | 72-74 | 3 | |
| α-helix | 75-87 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Glucose-specific phosphotransferase enzyme IIB component | A, B | protein | 82 | Escherichia coli | P69786 (AlphaFold model) |
>3BP3_1 Glucose-specific phosphotransferase enzyme IIB component (chains A, B) TGTSEMAPALVAAFGGKENITNLDACITRLRVSVADVSKVDQAGLKKLGAAGVVVAGSGV QAIFGTKSDNLKTEMDEYIRNH
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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