MolNFT v1 · #138219 · protein
Crystal structure of ADP-bound human TRIP13
5WC2 · Pachytene checkpoint protein 2 homolog: “Crystal structure of ADP-bound human TRIP13”. X-ray diffraction, 1 ligand (ADP), 3 pockets (best druggability 0.56). MolNFT v1 #138219 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 5WC2
- Type
- protein
- Length
- 364 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pachytene checkpoint protein 2 homolog
- UniProt
- Q15645
- Ligands
- ADP
- Pockets
- 3 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pachytene checkpoint protein 2 homolog | protein | 364 | 46% helix, 18% strand | Q15645 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 219 | 0.56 | 0.79 | 36 | empty |
| 2 | 95 | 0.53 | 0.83 | 21 | empty |
| 3 | 163 | 0.52 | 0.79 | 32 | ADP |
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 5WC2 · PDBe 5WC2 · UniProt Q15645
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