Research workbench
The cryo-EM structure of filamentous bacteriophage ike major coat protein P8 shell assembly.
Analyse The cryo-EM structure of filamentous bacteriophage ike major coat protein P8… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6A7F
- Type
- protein
- Length
- 1,410 residues
- Chains
- 30
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Major coat protein P8
- UniProt
- P03620
- Pockets
- 20 · best druggability 0.51
Structure
electron microscopy · 1 distinct chain · 91% helix, 0% 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, V, W, X, Y, Z, a, b, c, d | Major coat protein P8 | protein | 47 | 91% helix, 0% strand | P03620 |
Pockets
20 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 200 | 0.51 | 0.76 | 20 | empty |
| 2 | 169 | 0.49 | 0.76 | 14 | empty |
| 3 | 178 | 0.48 | 0.75 | 21 | empty |
| 4 | 158 | 0.48 | 0.76 | 20 | empty |
| 5 | 141 | 0.45 | 0.76 | 15 | empty |
Interfaces
113 interfaces between chains.
- I–N · 811 Ų buried · 2 hydrogen bonds · protein-protein
- R–W · 798 Ų buried · 2 hydrogen bonds · protein-protein
- U–Z · 797 Ų buried · 3 hydrogen bonds · protein-protein
- T–Y · 794 Ų buried · 3 hydrogen bonds · protein-protein
- J–O · 792 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 6A7F · The cryo-EM structure of filamentous bacteriophage IKe major coat protein p8 shell… · the same entry in another collection · chain B against B, 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 P03620
- Elsewhere: RCSB PDB 6A7F · PDBe 6A7F · UniProt P03620
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