Research workbench
Crystal structure of gravn
Analyse Crystal structure of gravn in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4J4X
- Type
- protein
- Length
- 1,491 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Np protein
- UniProt
- E2DQZ4
- Pockets
- 12 · best druggability 0.82
Structure
x-ray diffraction · 5 distinct chains · 69% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Np protein | protein | 250 | 68% helix, 1% strand | E2DQZ4 |
| B, F | Np protein | protein | 248 | 71% helix, 1% strand | E2DQZ4 |
| C | Np protein | protein | 246 | 67% helix, 1% strand | E2DQZ4 |
| D | Np protein | protein | 249 | 68% helix, 1% strand | E2DQZ4 |
| E | Np protein | protein | 250 | 70% helix, 2% strand | E2DQZ4 |
Pockets
12 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 853 | 0.82 | 0.84 | 93 | empty |
| 2 | 668 | 0.80 | 0.85 | 81 | empty |
| 3 | 547 | 0.78 | 0.85 | 66 | empty |
| 4 | 361 | 0.74 | 0.85 | 46 | empty |
| 5 | 376 | 0.74 | 0.85 | 50 | empty |
Interfaces
6 interfaces between chains.
- D–E · 1831 Ų buried · 19 hydrogen bonds · protein-protein
- A–F · 1773 Ų buried · 20 hydrogen bonds · protein-protein
- B–C · 1718 Ų buried · 16 hydrogen bonds · protein-protein
- A–B · 1628 Ų buried · 20 hydrogen bonds · protein-protein
- C–D · 1588 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 4J4X · Crystal structure of GraVN · 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 E2DQZ4
- Elsewhere: RCSB PDB 4J4X · PDBe 4J4X · UniProt E2DQZ4
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