Research workbench
Importin binding to pol mu nls peptide
Analyse Importin binding to pol mu nls peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5W4F
- Type
- protein
- Length
- 437 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Importin subunit alpha-1; DNA-directed DNA/RNA polymerase mu
- EC
- 2.7.7.7
- UniProt
- P52293, Q9NP87
- Pockets
- 1 · best druggability 0.44
Structure
x-ray diffraction · 3 distinct chains · 72% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Importin subunit alpha-1 | protein | 425 | 74% helix, 0% strand | P52293 |
| A | DNA-directed DNA/RNA polymerase mu (EC 2.7.7.7) | protein | 7 | 0% helix, 0% strand | Q9NP87 |
| D | DNA-directed DNA/RNA polymerase mu (EC 2.7.7.7) | protein | 5 | 0% helix, 0% strand | Q9NP87 |
Ligands and binding sites
- GOL · Glycerol · additive · 2 copies · chains B
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 | 70 | 0.44 | 0.81 | 12 | empty |
Interfaces
2 interfaces between chains.
- B–A · 719 Ų buried · 20 hydrogen bonds · protein-protein
- B–D · 564 Ų buried · 17 hydrogen bonds · protein-protein
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 P52293
- Every structure of UniProt Q9NP87
- Elsewhere: RCSB PDB 5W4F · PDBe 5W4F · UniProt P52293 · UniProt Q9NP87
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