Research workbench
The host outer membrane proteins ompa and ompc are packed at specific sites in the shigella phage SF6 virion as structural components
Analyse The host outer membrane proteins ompa and ompc are packed at specific sites in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3NB3
- Type
- protein
- Length
- 757 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Outer membrane protein a; Outer membrane protein C
- UniProt
- P0A910, P06996
- Pockets
- 5 · best druggability 0.69
Structure
electron microscopy · 2 distinct chains · 4% helix, 63% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Outer membrane protein a | protein | 137 | 0% helix, 78% strand | P0A910 |
| D | Outer membrane protein C | protein | 346 | 6% helix, 56% strand | P06996 |
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 895 | 0.69 | 0.75 | 68 | empty |
| 2 | 213 | 0.56 | 0.79 | 25 | empty |
| 3 | 199 | 0.53 | 0.78 | 25 | empty |
| 4 | 188 | 0.52 | 0.78 | 24 | empty |
| 5 | 193 | 0.44 | 0.73 | 33 | empty |
Compared structures
- 3NB3 · The host outer membrane proteins OmpA and OmpC are packed at specific sites in the… · the same entry in another collection · chain A against A, TM-score 1.00
- P06996 · AlphaFold monomer V2.0 prediction for outer membrane porin C (P06996) · a predicted model of the same protein · chain D against A, TM-score 0.99
- P0A910 · AlphaFold monomer V2.0 prediction for outer membrane protein a (P0A910) · a predicted model of the same protein · chain A against A, TM-score 0.93
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P0A910
- Every structure of UniProt P06996
- Elsewhere: RCSB PDB 3NB3 · PDBe 3NB3 · UniProt P0A910 · UniProt P06996
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