Research workbench
Crystal structure and X-ray diffraction data collection of importin- alpha from mus musculus complexed with a PMS2 nls peptide
Analyse Crystal structure and X-ray diffraction data collection of importin- alpha from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5U5R
- Type
- protein
- Length
- 437 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Importin subunit alpha-1; Mismatch repair endonuclease PMS2
- EC
- 3.1.-.-
- UniProt
- P52293, P54278
- Pockets
- 2 · best druggability 0.45
Structure
x-ray diffraction · 2 distinct chains · 73% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Importin subunit alpha-1 | protein | 426 | 74% helix, 0% strand | P52293 |
| B | Mismatch repair endonuclease PMS2 (EC 3.1.-.-) | protein | 11 | 0% helix, 0% strand | P54278 |
Ligands and binding sites
- DTT · 2,3-dihydroxy-1,4-dithiobutane · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 68 | 0.45 | 0.82 | 12 | empty |
| 2 | 61 | 0.29 | 0.74 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 780 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 5U5R · Crystal Structure and X-ray Diffraction Data Collection of Importin-alpha from Mus… · the same entry in another collection · chain A against A, TM-score 1.00
- P54278 · AlphaFold monomer V2.0 prediction for mismatch repair endonuclease PMS2 (P54278) · a predicted model of the same protein · chain B against A, TM-score 0.44
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 P52293
- Every structure of UniProt P54278
- Elsewhere: RCSB PDB 5U5R · PDBe 5U5R · UniProt P52293 · UniProt P54278
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