Research workbench
Crystal structure of human DBP5 in complex with NUP214
Analyse Crystal structure of human DBP5 in complex with NUP214 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3FHC
- Type
- protein
- Length
- 605 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nuclear pore complex protein NUP214; ATP-dependent RNA helicase DDX19B
- EC
- 3.6.1.-
- UniProt
- P35658, Q9UMR2
- Pockets
- 9 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 18% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nuclear pore complex protein NUP214 | protein | 381 | 5% helix, 48% strand | P35658 |
| B | ATP-dependent RNA helicase DDX19B (EC 3.6.1.-) | protein | 224 | 40% helix, 16% strand | Q9UMR2 |
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 738 | 0.77 | 0.81 | 49 | empty |
| 2 | 69 | 0.58 | 0.89 | 16 | empty |
| 3 | 106 | 0.52 | 0.82 | 23 | empty |
| 4 | 148 | 0.52 | 0.79 | 25 | empty |
| 5 | 109 | 0.49 | 0.81 | 28 | empty |
Interfaces
1 interface between chains.
- A–B · 1157 Ų buried · 33 hydrogen bonds · protein-protein
Compared structures
- 3FHC · Crystal structure of human Dbp5 in complex with Nup214 · the same entry in another collection · chain A against A, TM-score 1.00
- P35658 · AlphaFold monomer V2.0 prediction for nuclear pore complex protein NUP214 (P35658) · a predicted model of the same protein · chain A against A, TM-score 0.99
- Q9UMR2 · AlphaFold monomer V2.0 prediction for ATP-dependent RNA helicase DDX19B (Q9UMR2) · a predicted model of the same protein · chain B against A, TM-score 0.97
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 P35658
- Every structure of UniProt Q9UMR2
- Elsewhere: RCSB PDB 3FHC · PDBe 3FHC · UniProt P35658 · UniProt Q9UMR2
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