Structure of MoeN5-Sso7d fusion protein in complex with beta-octyl glucoside. Determined by X-ray diffraction at 2.26 Å resolution. Released 23 Mar 2016.
Explore 5B0I in 3D Show helices and sheets RCSB PDB PDBe
5B0I contains 68 α-helices and 10 β-strands across 4 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 | -3-18 | 22 | |
| α-helix | 23-30 | 8 | |
| α-helix | 33-42 | 10 | |
| α-helix | 49-74 | 26 | |
| α-helix | 81-102 | 22 | |
| α-helix | 107-115 | 9 | |
| α-helix | 117-129 | 13 | |
| α-helix | 135-142 | 8 | |
| α-helix | 143-148 | 6 | |
| α-helix | 149-160 | 12 | |
| α-helix | 167-189 | 23 | |
| α-helix | 200-205 | 6 | |
| α-helix | 211-230 | 20 | |
| α-helix | 238-248 | 11 | |
| α-helix | 249-253 | 5 | |
| α-helix | 254-257 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | -3-18 | 22 | |
| α-helix | 23-31 | 9 | |
| α-helix | 33-42 | 10 | |
| α-helix | 49-74 | 26 | |
| α-helix | 81-102 | 22 | |
| α-helix | 108-115 | 8 | |
| α-helix | 117-129 | 13 | |
| α-helix | 135-142 | 8 | |
| α-helix | 143-148 | 6 | |
| α-helix | 149-160 | 12 | |
| α-helix | 167-189 | 23 | |
| α-helix | 200-205 | 6 | |
| α-helix | 211-230 | 20 | |
| α-helix | 238-248 | 11 | |
| α-helix | 249-253 | 5 | |
| α-helix | 255-258 | 4 | |
| β-strand | 268-271 | 4 | 1 |
| β-strand | 278-281 | 4 | 1 |
| β-strand | 285-291 | 7 | 2 |
| β-strand | 294-300 | 7 | 2 |
| β-strand | 306-312 | 7 | 2 |
| α-helix | 313-315 | 3 | |
| α-helix | 318-325 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | -1-18 | 20 | |
| α-helix | 23-30 | 8 | |
| α-helix | 33-42 | 10 | |
| α-helix | 49-74 | 26 | |
| α-helix | 81-102 | 22 | |
| α-helix | 106-115 | 10 | |
| α-helix | 117-128 | 12 | |
| α-helix | 135-142 | 8 | |
| α-helix | 143-147 | 5 | |
| α-helix | 148-161 | 14 | |
| α-helix | 167-193 | 27 | |
| α-helix | 200-206 | 7 | |
| α-helix | 211-230 | 20 | |
| α-helix | 238-248 | 11 | |
| α-helix | 249-253 | 5 | |
| α-helix | 254-257 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | -2-18 | 21 | |
| α-helix | 23-30 | 8 | |
| α-helix | 33-42 | 10 | |
| α-helix | 49-74 | 26 | |
| α-helix | 81-102 | 22 | |
| α-helix | 108-115 | 8 | |
| α-helix | 117-129 | 13 | |
| α-helix | 135-142 | 8 | |
| α-helix | 143-148 | 6 | |
| α-helix | 149-160 | 12 | |
| α-helix | 167-192 | 26 | |
| α-helix | 200-205 | 6 | |
| α-helix | 211-230 | 20 | |
| α-helix | 238-248 | 11 | |
| α-helix | 249-253 | 5 | |
| α-helix | 254-257 | 4 | |
| β-strand | 268-273 | 6 | 3 |
| β-strand | 276-281 | 6 | 3 |
| α-helix | 282-284 | 3 | |
| β-strand | 285-291 | 7 | 4 |
| β-strand | 294-300 | 7 | 4 |
| β-strand | 306-312 | 7 | 4 |
| α-helix | 320-324 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| MoeN5,DNA-binding protein 7d | A, B, C, D | protein | 343 | Streptomyces ghanaensis, Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) | A0A010 (AlphaFold model), P39476 (AlphaFold model) |
>5B0I_1 MoeN5,DNA-binding protein 7d (chains A, B, C, D) MAHHHHHHVDDDDKMLAAEAANRDHVTRCVAQTGGSPDLVAHTAALRLYLRVPHFLTEWT TDPDRRAAVSRALALDIVSMKLLDDLMDDDTGLDRVELACVCLRLHLRALHELESLARDP KAVTDILEQDAVHLCGGQIRTKRSRATNLREWRAHASTYGSTFLGRYGALAAACGGEGQP ADSVREFAEAFAMTITMADDLTDYDRNGERDGNLAHLMRTGAVAGQDVVDLLEELRGRAL AAVAAPPGAPGLVPVVHLYTDDVLVRLLPRHLGEAGAGAMATVKFKYKGEEKEVDISKIK KVWRVGKMISFTYDEGGGKTGRGAVSEKDAPKELLQMLEKQKK
| ID | Name | Formula | Copies |
|---|---|---|---|
| BOG | octyl beta-D-glucopyranoside | C14 H28 O6 | 5 |
Moenomycin Biosynthesis: Structure and Mechanism of Action of the Prenyltransferase MoeN5. Zhang, L., Chen, C.C., Ko, T.P. et al. Angew Chem Int Ed Engl (2016) 55:4716-4720. DOI 10.1002/anie.201511388 · PubMed
Other PDB entries of the same protein (UniProt A0A010 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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