MolNFT v1 · #137492 · protein
Structure of human TRIP13, ATP-bound form
5VQA · Pachytene checkpoint protein 2 homolog: “Structure of human TRIP13, ATP-bound form”. X-ray diffraction, 1 ligand (ATP), 4 pockets (best druggability 0.57). MolNFT v1 #137492 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 5VQA
- Type
- protein
- Length
- 368 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pachytene checkpoint protein 2 homolog
- UniProt
- Q15645
- Ligands
- ATP
- Pockets
- 4 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pachytene checkpoint protein 2 homolog | protein | 368 | 46% helix, 17% strand | Q15645 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 309 | 0.57 | 0.76 | 37 | empty |
| 2 | 124 | 0.54 | 0.82 | 29 | empty |
| 3 | 158 | 0.50 | 0.78 | 32 | ATP |
| 4 | 142 | 0.49 | 0.78 | 23 | 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 5VQA · PDBe 5VQA · UniProt Q15645
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