Research workbench
Core proteins
Analyse Core proteins in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7EYB
- Type
- protein
- Length
- 10,204 residues
- Chains
- 20
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Internal virion protein GP14; Internal virion protein GP15; Peptidoglycan…
- EC
- 4.2.2.-
- UniProt
- P03724, P03725, P03726
- Pockets
- 20 · best druggability 0.87
Structure
electron microscopy · 3 distinct chains · 59% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| a, b, c, d, e, f, g, h | Internal virion protein GP14 | protein | 78 | 68% helix, 0% strand | P03724 |
| A, B, C, D, E, F, G, H | Internal virion protein GP15 | protein | 647 | 67% helix, 4% strand | P03725 |
| I, J, K, L | Peptidoglycan transglycosylase GP16 (EC 4.2.2.-) | protein | 1101 | 54% helix, 1% strand | P03726 |
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 | 1057 | 0.87 | 0.88 | 110 | empty |
| 2 | 1013 | 0.86 | 0.87 | 108 | empty |
| 3 | 903 | 0.85 | 0.86 | 106 | empty |
| 4 | 598 | 0.84 | 0.89 | 76 | empty |
| 5 | 1097 | 0.83 | 0.84 | 111 | empty |
Interfaces
72 interfaces between chains.
- A–H · 4422 Ų buried · 38 hydrogen bonds · protein-protein
- F–G · 4410 Ų buried · 38 hydrogen bonds · protein-protein
- D–E · 4403 Ų buried · 37 hydrogen bonds · protein-protein
- B–C · 4352 Ų buried · 37 hydrogen bonds · protein-protein
- A–B · 4072 Ų buried · 31 hydrogen bonds · protein-protein
Compared structures
- 7EYB · core proteins · the same entry in another collection · chain f against f, 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 P03724
- Every structure of UniProt P03725
- Every structure of UniProt P03726
- Elsewhere: RCSB PDB 7EYB · PDBe 7EYB · UniProt P03724 · UniProt P03725 · UniProt P03726
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