Research workbench
Crystal structure and X-ray diffraction data collection of importin- alpha from mus musculus complexed with a MLH1 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
- 5U5P
- Type
- protein
- Length
- 445 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA mismatch repair protein MLH1; Importin subunit alpha-1
- UniProt
- P40692, P52293
- Pockets
- 1 · best druggability 0.47
Structure
x-ray diffraction · 3 distinct chains · 70% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | DNA mismatch repair protein MLH1 | protein | 9 | 0% helix, 0% strand | P40692 |
| B | DNA mismatch repair protein MLH1 | protein | 10 | 0% helix, 0% strand | P40692 |
| A | Importin subunit alpha-1 | protein | 426 | 73% helix, 0% strand | P52293 |
Ligands and binding sites
- DTT · 2,3-dihydroxy-1,4-dithiobutane · additive · chains B, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 80 | 0.47 | 0.82 | 13 | empty |
Interfaces
2 interfaces between chains.
- B–A · 830 Ų buried · 21 hydrogen bonds · protein-protein
- C–A · 665 Ų buried · 20 hydrogen bonds · protein-protein
Compared structures
- 5U5P · Crystal Structure and X-ray Diffraction Data Collection of Importin-alpha from Mus… · the same entry in another collection · chain C against C, TM-score 1.00
- P40692 · AlphaFold monomer V2.0 prediction for DNA mismatch repair protein MLH1 (P40692) · a predicted model of the same protein · chain C against A, TM-score 0.51
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 P40692
- Every structure of UniProt P52293
- Elsewhere: RCSB PDB 5U5P · PDBe 5U5P · UniProt P40692 · UniProt P52293
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