Research workbench
Improved refinement of the MTR4 apo crystal structure
Analyse Improved refinement of the MTR4 apo crystal structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4QU4
- Type
- protein
- Length
- 942 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-dependent RNA helicase DOB1
- EC
- 3.6.4.13
- UniProt
- P47047
- Ligands
- PO4
- Pockets
- 11 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent RNA helicase DOB1 (EC 3.6.4.13) | protein | 942 | 38% helix, 16% strand | P47047 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1023 | 0.80 | 0.81 | 107 | empty |
| 2 | 917 | 0.77 | 0.80 | 85 | PO4 |
| 3 | 608 | 0.74 | 0.81 | 51 | empty |
| 4 | 115 | 0.67 | 0.90 | 22 | empty |
| 5 | 298 | 0.63 | 0.80 | 47 | 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 P47047
- Elsewhere: RCSB PDB 4QU4 · PDBe 4QU4 · UniProt P47047
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