Research workbench
Fitting of GP8, GP9, and GP11 into the cryo-EM reconstruction of the bacteriophage T4 contracted tail
Analyse Fitting of GP8, GP9, and GP11 into the cryo-EM reconstruction of the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TJA
- Type
- protein
- Length
- 2,144 residues
- Chains
- 8
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Baseplate structural protein GP8; Baseplate structural protein GP9; Baseplate structural…
- UniProt
- P19062, P10927, P10929
- Pockets
- 5 · best druggability 0.37
Structure
electron microscopy · 3 distinct chains · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Baseplate structural protein GP8 | protein | 328 | 0% helix, 0% strand | P19062 |
| C, D, E | Baseplate structural protein GP9 | protein | 288 | 0% helix, 0% strand | P10927 |
| F, G, H | Baseplate structural protein GP11 | protein | 208 | 0% helix, 0% strand | P10929 |
Pockets
5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 101 | 0.37 | 0.72 | 28 | empty |
| 2 | 88 | 0.34 | 0.72 | 27 | empty |
| 3 | 79 | 0.33 | 0.72 | 22 | empty |
| 4 | 66 | 0.30 | 0.72 | 18 | empty |
| 5 | 60 | 0.30 | 0.73 | 23 | empty |
Interfaces
8 interfaces between chains.
- A–B · 385 Ų buried · 0 hydrogen bonds · protein-protein
- C–E · 382 Ų buried · 0 hydrogen bonds · protein-protein
- D–E · 380 Ų buried · 0 hydrogen bonds · protein-protein
- C–D · 379 Ų buried · 0 hydrogen bonds · protein-protein
- F–G · 325 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 1TJA · Fitting of gp8, gp9, and gp11 into the cryo-EM reconstruction of the bacteriophage T4… · 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 P19062
- Every structure of UniProt P10927
- Every structure of UniProt P10929
- Elsewhere: RCSB PDB 1TJA · PDBe 1TJA · UniProt P19062 · UniProt P10927 · UniProt P10929
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