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Crystal structure of human wild type TRIP13
Analyse Crystal structure of human wild type TRIP13 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6LK0
- Type
- protein
- Length
- 336 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pachytene checkpoint protein 2 homolog
- UniProt
- Q15645
- Pockets
- 6 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pachytene checkpoint protein 2 homolog | protein | 336 | 45% helix, 18% strand | Q15645 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 152 | 0.57 | 0.82 | 25 | empty |
| 2 | 117 | 0.53 | 0.82 | 20 | empty |
| 3 | 135 | 0.47 | 0.78 | 24 | empty |
| 4 | 207 | 0.45 | 0.73 | 31 | empty |
| 5 | 59 | 0.33 | 0.77 | 14 | empty |
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 Q15645
- Elsewhere: RCSB PDB 6LK0 · PDBe 6LK0 · UniProt Q15645
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