MolNFT v1 · #117847 · protein
Crystallization and X-ray diffraction data collection of importin- alpha from mus musculus complexed with a xpg nls peptide, fragment 1
5EKF · DNA repair protein complementing xp-G cells: “Crystallization and X-ray diffraction data collection of importin- alpha from mus musculus complexed with a…”. X-ray diffraction, 2 pockets (best druggability 0.50). MolNFT v1 #117847 on…
- PDB
- 5EKF
- Type
- protein
- Length
- 441 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA repair protein complementing xp-G cells; Importin subunit alpha-1
- UniProt
- P28715, P52293
- Pockets
- 2 · best druggability 0.50
Structure
x-ray diffraction · 3 distinct chains · 72% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | DNA repair protein complementing xp-G cells | protein | 6 | 0% helix, 0% strand | P28715 |
| C | DNA repair protein complementing xp-G cells | protein | 10 | 0% helix, 0% strand | P28715 |
| A | Importin subunit alpha-1 | protein | 425 | 75% helix, 0% strand | P52293 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 73 | 0.50 | 0.84 | 19 | empty |
| 2 | 50 | 0.29 | 0.76 | 12 | empty |
Interfaces
2 interfaces between chains.
- C–A · 816 Ų buried · 22 hydrogen bonds · protein-protein
- B–A · 579 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 5EKF · Crystallization and X-ray Diffraction Data Collection of Importin-alpha from Mus musculus… · the same entry in another collection · chain B against B, TM-score 1.00
- P28715 · AlphaFold monomer V2.0 prediction for DNA repair protein complementing xp-G cells (P28715) · a predicted model of the same protein · chain B against A, TM-score 0.71
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 P28715
- Every structure of UniProt P52293
- Elsewhere: RCSB PDB 5EKF · PDBe 5EKF · UniProt P28715 · UniProt P52293
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