Research workbench
Filament of octameric rings of DMC1 recombinase from homo sapiens
Analyse Filament of octameric rings of DMC1 recombinase from homo sapiens in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4HYY
- Type
- protein
- Length
- 964 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Meiotic recombination protein DMC1/LIM15 homolog
- UniProt
- Q14565
- Pockets
- 10 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Meiotic recombination protein DMC1/LIM15 homolog | protein | 241 | 41% helix, 27% strand | Q14565 |
Pockets
10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 717 | 0.70 | 0.77 | 49 | empty |
| 2 | 779 | 0.69 | 0.76 | 48 | empty |
| 3 | 377 | 0.59 | 0.75 | 42 | empty |
| 4 | 290 | 0.52 | 0.74 | 29 | empty |
| 5 | 83 | 0.45 | 0.81 | 26 | empty |
Interfaces
5 interfaces between chains.
- A–B · 1289 Ų buried · 17 hydrogen bonds · protein-protein
- C–D · 1255 Ų buried · 16 hydrogen bonds · protein-protein
- B–D · 259 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 249 Ų buried · 5 hydrogen bonds · protein-protein
- A–D · 243 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 4HYY · Filament of octameric rings of DMC1 recombinase from Homo sapiens · the same entry in another collection · chain D against D, TM-score 1.00
- Q14565 · AlphaFold monomer V2.0 prediction for meiotic recombination protein DMC1/LIM15 homolog… · a predicted model of the same protein · chain A against A, TM-score 0.95
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 Q14565
- Elsewhere: RCSB PDB 4HYY · PDBe 4HYY · UniProt Q14565
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