Research workbench
Human karyopherin RANBP5 (isoform-3)
Analyse Human karyopherin RANBP5 (isoform-3) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6XU2
- Type
- protein
- Length
- 1,093 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Importin-5; Antipain
- UniProt
- O00410
- Ligands
- FC0, OAR, NI
- Pockets
- 12 · best druggability 0.60
Structure
x-ray diffraction · 2 distinct chains · 75% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Importin-5 | protein | 1091 | 75% helix, 1% strand | O00410 |
| G | Antipain | protein | 2 | 0% helix, 0% strand | — |
Ligands and binding sites
- FC0 · N-carboxy-L-phenylalanine · ligand · chains A, G
- OAR · N-(4-amino-5-hydroxy-pentyl)-guanidine · ligand · chains A, G
- NI · Nickel (II) ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 440 | 0.60 | 0.75 | 51 | empty |
| 2 | 249 | 0.57 | 0.79 | 33 | OAR |
| 3 | 80 | 0.53 | 0.84 | 14 | empty |
| 4 | 116 | 0.51 | 0.81 | 21 | empty |
| 5 | 138 | 0.48 | 0.78 | 24 | empty |
Interfaces
1 interface between chains.
- A–G · 174 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 2 covalent (covalent ligand).
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 O00410
- Elsewhere: RCSB PDB 6XU2 · PDBe 6XU2 · UniProt O00410
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