5B0M: MoeN5-Sso7d fusion protein
Structure of MoeN5-Sso7d fusion protein in complex with beta-dodecyl maltoside. Determined by X-ray diffraction at 3.05 Å resolution. Released 23 Mar 2016.
- Method
- X-ray diffraction
- Resolution
- 3.05 Å
- Organisms
- Streptomyces ghanaensis, Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
- Chains
- 8
- Atoms
- 19,074
- Mol. weight
- 304.74 kDa
- Ligands
- LMT
- Released
- 23 Mar 2016
Explore 5B0M in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
5B0M contains 133 α-helices and 20 β-strands across 8 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: 16 helices, 0 β-strands
| 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 | 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 | 167-187 | 21 | |
| α-helix | 199-206 | 8 | |
| α-helix | 211-230 | 20 | |
| α-helix | 238-247 | 10 | |
| α-helix | 248-253 | 6 | |
| α-helix | 254-257 | 4 | |
Chain B: 19 helices, 5 β-strands
| 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 | 117-127 | 11 | |
| α-helix | 135-142 | 8 | |
| α-helix | 143-148 | 6 | |
| α-helix | 149-160 | 12 | |
| α-helix | 167-187 | 21 | |
| α-helix | 196-198 | 3 | |
| α-helix | 199-205 | 7 | |
| α-helix | 211-228 | 18 | |
| α-helix | 238-247 | 10 | |
| α-helix | 248-253 | 6 | |
| α-helix | 254-257 | 4 | |
| β-strand | 268-271 | 4 | 1 |
| β-strand | 278-281 | 4 | 1 |
| α-helix | 282-284 | 3 | |
| β-strand | 285-291 | 7 | 2 |
| β-strand | 294-300 | 7 | 2 |
| β-strand | 306-312 | 7 | 2 |
| α-helix | 318-327 | 10 | |
Chain C: 16 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | -3-18 | 22 | |
| α-helix | 23-30 | 8 | |
| α-helix | 33-43 | 11 | |
| α-helix | 49-74 | 26 | |
| α-helix | 81-100 | 20 | |
| 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 | 167-186 | 20 | |
| α-helix | 199-205 | 7 | |
| α-helix | 211-228 | 18 | |
| α-helix | 238-248 | 11 | |
| α-helix | 249-253 | 5 | |
| α-helix | 254-257 | 4 | |
Chain D: 17 helices, 5 β-strands
| 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 | 81-100 | 20 | |
| α-helix | 108-115 | 8 | |
| α-helix | 117-129 | 13 | |
| α-helix | 135-141 | 7 | |
| α-helix | 142-148 | 7 | |
| α-helix | 149-160 | 12 | |
| α-helix | 167-186 | 20 | |
| α-helix | 199-204 | 6 | |
| α-helix | 211-230 | 20 | |
| α-helix | 238-248 | 11 | |
| α-helix | 249-253 | 5 | |
| α-helix | 254-257 | 4 | |
| β-strand | 268-271 | 4 | 3 |
| β-strand | 278-281 | 4 | 3 |
| β-strand | 285-291 | 7 | 4 |
| β-strand | 294-302 | 9 | 4 |
| β-strand | 305-312 | 8 | 4 |
| α-helix | 318-326 | 9 | |
Chain E: 15 helices, 0 β-strands
| 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 | 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 | 167-192 | 26 | |
| α-helix | 200-206 | 7 | |
| α-helix | 211-230 | 20 | |
| α-helix | 238-248 | 11 | |
| α-helix | 249-253 | 5 | |
Chain F: 16 helices, 5 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 0-17 | 18 | |
| 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 | 200-206 | 7 | |
| α-helix | 211-230 | 20 | |
| α-helix | 238-248 | 11 | |
| α-helix | 249-253 | 5 | |
| β-strand | 268-273 | 6 | 5 |
| β-strand | 276-281 | 6 | 5 |
| β-strand | 285-291 | 7 | 6 |
| β-strand | 294-302 | 9 | 6 |
| β-strand | 305-312 | 8 | 6 |
| α-helix | 318-327 | 10 | |
Chain G: 16 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 0-17 | 18 | |
| α-helix | 23-30 | 8 | |
| α-helix | 33-42 | 10 | |
| α-helix | 49-74 | 26 | |
| α-helix | 81-100 | 20 | |
| 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 | 167-192 | 26 | |
| α-helix | 200-206 | 7 | |
| α-helix | 211-230 | 20 | |
| α-helix | 239-248 | 10 | |
| α-helix | 249-253 | 5 | |
| α-helix | 254-259 | 6 | |
Chain H: 18 helices, 5 β-strands
| 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 | 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 | 200-206 | 7 | |
| α-helix | 211-230 | 20 | |
| α-helix | 236-238 | 3 | |
| α-helix | 239-248 | 10 | |
| α-helix | 249-253 | 5 | |
| α-helix | 254-257 | 4 | |
| β-strand | 268-271 | 4 | 7 |
| β-strand | 278-281 | 4 | 7 |
| β-strand | 285-291 | 7 | 8 |
| β-strand | 294-302 | 9 | 8 |
| β-strand | 305-312 | 8 | 8 |
| α-helix | 318-327 | 10 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| MoeN5,DNA-binding protein 7d | A, B, C, D, E, F, G, H | protein | 343 | Streptomyces ghanaensis, Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) | A0A010 (AlphaFold model), P39476 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E, F, G, H), FASTA
>5B0M_1 MoeN5,DNA-binding protein 7d (chains A, B, C, D, E, F, G, H)
MAHHHHHHVDDDDKMLAAEAANRDHVTRCVAQTGGSPDLVAHTAALRLYLRVPHFLTEWT
TDPDRRAAVSRALALDIVSMKLLDDLMDDDTGLDRVELACVCLRLHLRALHELESLARDP
KAVTDILEQDAVHLCGGQIRTKRSRATNLREWRAHASTYGSTFLGRYGALAAACGGEGQP
ADSVREFAEAFAMTITMADDLTDYDRNGERDGNLAHLMRTGAVAGQDVVDLLEELRGRAL
AAVAAPPGAPGLVPVVHLYTDDVLVRLLPRHLGEAGAGAMATVKFKYKGEEKEVDISKIK
KVWRVGKMISFTYDEGGGKTGRGAVSEKDAPKELLQMLEKQKK
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| LMT | Dodecyl-beta-D-maltoside | C24 H46 O11 | 8 |
Primary citation
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:
- 5B02 2.21 Å, Structure of the prenyltransferase MoeN5 with a fusion protein tag of Sso7d
- 6J8V 2.23 Å, Structure of MOEN5-SSO7D fusion protein in complex with ligand 2
- 5B0I 2.26 Å, Structure of MoeN5-Sso7d fusion protein in complex with beta-octyl glucoside
- 5GWW 2.3 Å, Structure of MoeN5-Sso7d fusion protein in complex with a permethylated substrate analogue
- 6J8W 2.35 Å, Structure of MOEN5-SSO7D fusion protein in complex with lig 1
- 5GWV 2.4 Å, Structure of MoeN5-Sso7d fusion protein in complex with a substrate analogue
- 5B0J 2.5 Å, Structure of MoeN5-Sso7d fusion protein in complex with beta-undecyl maltoside
- 5B03 2.6 Å, Structure of MoeN5-Sso7d fusion protein in complex with geranyl pyrophosphate
- 5B0K 2.75 Å, Structure of MoeN5-Sso7d fusion protein in complex with beta-decyl maltoside
- 5B0L 2.8 Å, Structure of MoeN5-Sso7d fusion protein in complex with beta-nonyl glucoside
- 5B00 2.95 Å, Structure of the prenyltransferase MoeN5 in complex with geranyl pyrophosphate
- 5B01 3.45 Å, Structure of a prenyltransferase in its unbound form
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