Research workbench
Structure of NUP120
Analyse Structure of NUP120 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3F7F
- Type
- protein
- Length
- 2,804 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nucleoporin NUP120
- UniProt
- P35729
- Ligands
- HG
- Pockets
- 20 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Nucleoporin NUP120 | protein | 701 | 32% helix, 26% strand | P35729 |
Ligands and binding sites
- HG · Mercury (II) ion · metal · 12 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 784 | 0.78 | 0.82 | 92 | empty |
| 2 | 750 | 0.77 | 0.82 | 85 | empty |
| 3 | 91 | 0.75 | 0.97 | 23 | empty |
| 4 | 87 | 0.74 | 0.97 | 22 | empty |
| 5 | 333 | 0.72 | 0.85 | 43 | empty |
Interfaces
5 interfaces between chains.
- A–B · 1583 Ų buried · 17 hydrogen bonds · protein-protein
- B–C · 647 Ų buried · 4 hydrogen bonds · protein-protein
- C–D · 191 Ų buried · 1 hydrogen bond · protein-protein
- A–C · 189 Ų buried · 1 hydrogen bond · protein-protein
- B–D · 179 Ų buried · 1 hydrogen bond · 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 P35729
- Elsewhere: RCSB PDB 3F7F · PDBe 3F7F · UniProt P35729
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