Research workbench
Asymmetric unit for phage qbeta prolate particle
Analyse Asymmetric unit for phage qbeta prolate particle in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7LGF
- Type
- protein
- Length
- 2,772 residues
- Chains
- 21
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Capsid protein
- UniProt
- P03615
- Pockets
- 20 · best druggability 0.70
Structure
electron microscopy · 1 distinct chain · 20% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U | Capsid protein | protein | 132 | 20% helix, 40% strand | P03615 |
Pockets
20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 56 | 0.70 | 0.97 | 23 | empty |
| 2 | 776 | 0.68 | 0.75 | 87 | empty |
| 3 | 463 | 0.68 | 0.79 | 60 | empty |
| 4 | 371 | 0.67 | 0.81 | 46 | empty |
| 5 | 306 | 0.67 | 0.83 | 40 | empty |
Interfaces
56 interfaces between chains.
- E–O · 3580 Ų buried · 42 hydrogen bonds · protein-protein
- I–S · 3523 Ų buried · 38 hydrogen bonds · protein-protein
- K–U · 3480 Ų buried · 43 hydrogen bonds · protein-protein
- J–T · 3424 Ų buried · 31 hydrogen bonds · protein-protein
- C–M · 3413 Ų buried · 47 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 14 disulfide (disulfide).
Compared structures
- 7LGF · Asymmetric unit for phage Qbeta prolate particle · the same entry in another collection · chain A against A, TM-score 1.00
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 P03615
- Elsewhere: RCSB PDB 7LGF · PDBe 7LGF · UniProt P03615
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