Research workbench
The X-ray structure of the GP15 hexamer and the model of the GP18 protein fitted into the cryo-EM reconstruction of the contracted T4 tail
Analyse The X-ray structure of the GP15 hexamer and the model of the GP18 protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3J2N
- Type
- protein
- Length
- 4,920 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tail connector protein GP15; Tail sheath protein GP18
- UniProt
- P11112, P13332
- Pockets
- 20 · best druggability 0.74
Structure
electron microscopy · 2 distinct chains · 26% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Tail connector protein GP15 | protein | 211 | 25% helix, 40% strand | P11112 |
| U, V, W, X, Y, Z | Tail sheath protein GP18 | protein | 609 | 27% helix, 25% strand | P13332 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 487 | 0.74 | 0.82 | 75 | empty |
| 2 | 648 | 0.71 | 0.79 | 73 | empty |
| 3 | 173 | 0.71 | 0.89 | 29 | empty |
| 4 | 604 | 0.71 | 0.79 | 67 | empty |
| 5 | 165 | 0.70 | 0.89 | 32 | empty |
Interfaces
11 interfaces between chains.
- A–B · 1196 Ų buried · 15 hydrogen bonds · protein-protein
- A–F · 1192 Ų buried · 12 hydrogen bonds · protein-protein
- B–C · 1192 Ų buried · 12 hydrogen bonds · protein-protein
- E–F · 1190 Ų buried · 13 hydrogen bonds · protein-protein
- C–D · 1187 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 3J2N · The X-ray structure of the gp15 hexamer and the model of the gp18 protein fitted into the… · 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 P11112
- Every structure of UniProt P13332
- Elsewhere: RCSB PDB 3J2N · PDBe 3J2N · UniProt P11112 · UniProt P13332
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