Research workbench
Crystal structure of PRP43P in complex with ADP
Analyse Crystal structure of PRP43P in complex with ADP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3KX2
- Type
- protein
- Length
- 1,510 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP43
- EC
- 3.6.1.-
- UniProt
- P53131
- Ligands
- ADP, MG
- Pockets
- 20 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, A | Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP43 (EC 3.6.1.-) | protein | 755 | 44% helix, 16% strand | P53131 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains B, A
- MG · Magnesium ion · metal · 2 copies · chains B, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1029 | 0.84 | 0.85 | 86 | empty |
| 2 | 747 | 0.80 | 0.84 | 84 | empty |
| 3 | 1196 | 0.80 | 0.82 | 101 | empty |
| 4 | 287 | 0.70 | 0.85 | 34 | MG, ADP |
| 5 | 302 | 0.69 | 0.84 | 37 | MG, ADP |
Interfaces
1 interface between chains.
- B–A · 924 Ų buried · 22 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 P53131
- Elsewhere: RCSB PDB 3KX2 · PDBe 3KX2 · UniProt P53131
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.