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Crystal structure of the chromo domain of human MRG15
Analyse Crystal structure of the chromo domain of human MRG15 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2F5K
- Type
- protein
- Length
- 483 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mortality factor 4-like protein 1
- UniProt
- Q9UBU8
- Pockets
- 7 · best druggability 0.80
Structure
x-ray diffraction · 6 distinct chains · 29% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mortality factor 4-like protein 1 | protein | 83 | 31% helix, 39% strand | Q9UBU8 |
| B | Mortality factor 4-like protein 1 | protein | 85 | 28% helix, 40% strand | Q9UBU8 |
| C | Mortality factor 4-like protein 1 | protein | 80 | 30% helix, 36% strand | Q9UBU8 |
| D | Mortality factor 4-like protein 1 | protein | 79 | 28% helix, 41% strand | Q9UBU8 |
| E | Mortality factor 4-like protein 1 | protein | 78 | 27% helix, 38% strand | Q9UBU8 |
| F | Mortality factor 4-like protein 1 | protein | 78 | 32% helix, 37% strand | Q9UBU8 |
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 997 | 0.80 | 0.81 | 79 | empty |
| 2 | 763 | 0.79 | 0.83 | 63 | empty |
| 3 | 131 | 0.46 | 0.78 | 19 | empty |
| 4 | 87 | 0.44 | 0.80 | 14 | empty |
| 5 | 96 | 0.38 | 0.76 | 20 | empty |
Interfaces
7 interfaces between chains.
- A–C · 642 Ų buried · 6 hydrogen bonds · protein-protein
- B–D · 551 Ų buried · 3 hydrogen bonds · protein-protein
- D–F · 522 Ų buried · 3 hydrogen bonds · protein-protein
- A–E · 517 Ų buried · 3 hydrogen bonds · protein-protein
- C–E · 506 Ų buried · 6 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 Q9UBU8
- Elsewhere: RCSB PDB 2F5K · PDBe 2F5K · UniProt Q9UBU8
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