Structure of Shigella effector OspG in complex with host UbcH5c- Ubiquitin conjugate. Determined by X-ray diffraction at 2.7 Å resolution. Released 29 Jan 2014.
Explore 4BVU in 3D Show helices and sheets RCSB PDB PDBe
4BVU contains 14 α-helices and 25 β-strands across 3 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 |
|---|---|---|---|
| β-strand | 32-35 | 4 | 1 |
| β-strand | 39-43 | 5 | 1 |
| β-strand | 50-55 | 6 | 1 |
| α-helix | 62-80 | 19 | |
| β-strand | 85-90 | 6 | 1 |
| β-strand | 93-99 | 7 | 1 |
| β-strand | 104-105 | 2 | 2 |
| α-helix | 111-113 | 3 | |
| α-helix | 118-131 | 14 | |
| β-strand | 136 | 1 | 3 |
| α-helix | 141-143 | 3 | |
| β-strand | 144-147 | 4 | 2 |
| β-strand | 152-155 | 4 | 2 |
| β-strand | 160 | 1 | 3 |
| α-helix | 162-167 | 6 | |
| α-helix | 173-193 | 21 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-15 | 13 | |
| β-strand | 21-24 | 4 | 4 |
| β-strand | 32-38 | 7 | 4 |
| α-helix | 39-40 | 2 | |
| β-strand | 49-55 | 7 | 4 |
| β-strand | 66-69 | 4 | 4 |
| β-strand | 75 | 1 | 5 |
| β-strand | 78 | 1 | 5 |
| β-strand | 83 | 1 | 4 |
| β-strand | 84 | 1 | 5 |
| α-helix | 87-89 | 3 | |
| α-helix | 99-111 | 13 | |
| α-helix | 121-129 | 9 | |
| α-helix | 131-145 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 202-206 | 5 | 6 |
| β-strand | 212-216 | 5 | 6 |
| β-strand | 222 | 1 | 7 |
| α-helix | 223-234 | 12 | |
| α-helix | 238-240 | 3 | |
| β-strand | 241-244 | 4 | 6 |
| β-strand | 249 | 1 | 6 |
| β-strand | 255 | 1 | 7 |
| β-strand | 266-271 | 6 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein kinase ospg | A | protein | 211 | SHIGELLA FLEXNERI | Q99PZ6 (AlphaFold model) |
| Ubiquitin-conjugating enzyme E2 D3 | B | protein | 147 | HOMO SAPIENS | P61077 (AlphaFold model) |
| Ubiquitin | C | protein | 76 | HOMO SAPIENS | P0CG48 (AlphaFold model) |
>4BVU_1 PROTEIN KINASE OSPG (chains A) MGHHHHHHHHHHSSGMKITSTIIQTPFPFENNNSHAGIVTEPILGKLIGQGSTAEIFEDV NDSSALYKKYDLIGNQYNEILEMAWQESELFNAFYGDEASVVIQYGGDVYLRMLRVPGTP LSDIDTADIPDNIESLYLQLICKLNELSIIHYDLNTGNMLYDKESESLFPIDFRNIYAEY YAATKKDKEIIDRRLQMRTNDFYSLLNRKYL
>4BVU_2 UBIQUITIN-CONJUGATING ENZYME E2 D3 (chains B) MALKRINKELSDLARDPPAQCSAGPVGDDMFHWQATIMGPNDSPYQGGVFFLTIHFPTDY PFKPPKVAFTTRIYHPNINSNGSISLDILRSQWSPALTISKVLLSICSLLCDPNPDDPLV PEIARIYKTDRDKYNRISREWTQKYAM
>4BVU_3 UBIQUITIN (chains C) MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN IQKESTLHLVLRLRGG
E2~Ub Conjugates Regulate the Kinase Activity of Shigella Effector Ospg During Pathogenesis. Pruneda, J.N., Smith, F.D., Daurie, A. et al. EMBO J (2014) 33:437. DOI 10.1002/EMBJ.201386386 · PubMed
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