MolNFT v1 · #153023 · protein
Crystal structure of yeast RTT107 and MMS22
6J0X · Regulator of TY1 transposition protein 107: “Crystal structure of yeast RTT107 and MMS22”. X-ray diffraction, 20 pockets (best druggability 0.84). MolNFT v1 #153023 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6J0X
- Type
- protein
- Length
- 1,920 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Regulator of TY1 transposition protein 107; Peptide from E3 ubiquitin-protein ligase…
- UniProt
- P38850, Q06164
- Pockets
- 20 · best druggability 0.84
Structure
x-ray diffraction · 5 distinct chains · 39% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Regulator of TY1 transposition protein 107 | protein | 465 | 39% helix, 13% strand | P38850 |
| E, F, G, H | Peptide from E3 ubiquitin-protein ligase substrate receptor MMS22 | protein | 16 | 19% helix, 19% strand | Q06164 |
| B | Regulator of TY1 transposition protein 107 | protein | 466 | 38% helix, 14% strand | P38850 |
| C | Regulator of TY1 transposition protein 107 | protein | 463 | 40% helix, 14% strand | P38850 |
| D | Regulator of TY1 transposition protein 107 | protein | 462 | 39% helix, 14% strand | P38850 |
Pockets
20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1156 | 0.84 | 0.85 | 117 | empty |
| 2 | 99 | 0.79 | 0.99 | 18 | empty |
| 3 | 103 | 0.79 | 0.98 | 19 | empty |
| 4 | 95 | 0.79 | 0.99 | 17 | empty |
| 5 | 97 | 0.78 | 0.98 | 19 | empty |
Interfaces
7 interfaces between chains.
- A–B · 1134 Ų buried · 14 hydrogen bonds · protein-protein
- A–E · 966 Ų buried · 17 hydrogen bonds · protein-protein
- C–G · 955 Ų buried · 16 hydrogen bonds · protein-protein
- B–F · 950 Ų buried · 18 hydrogen bonds · protein-protein
- D–H · 940 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
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 P38850
- Every structure of UniProt Q06164
- Elsewhere: RCSB PDB 6J0X · PDBe 6J0X · UniProt P38850 · UniProt Q06164
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