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Crystal structure of the forkhead domain of human FOXN1
Analyse Crystal structure of the forkhead domain of human FOXN1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5OCN
- Type
- protein
- Length
- 664 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Forkhead box protein N1
- UniProt
- O15353
- Ligands
- K
- Pockets
- 7 · best druggability 0.68
Structure
x-ray diffraction · 7 distinct chains · 58% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Forkhead box protein N1 | protein | 86 | 58% helix, 13% strand | O15353 |
| B | Forkhead box protein N1 | protein | 87 | 57% helix, 14% strand | O15353 |
| C | Forkhead box protein N1 | protein | 83 | 60% helix, 13% strand | O15353 |
| D | Forkhead box protein N1 | protein | 82 | 55% helix, 13% strand | O15353 |
| E | Forkhead box protein N1 | protein | 82 | 59% helix, 15% strand | O15353 |
| F | Forkhead box protein N1 | protein | 84 | 56% helix, 13% strand | O15353 |
| G, H | Forkhead box protein N1 | protein | 80 | 59% helix, 14% strand | O15353 |
Ligands and binding sites
- K · Potassium ion · metal · 8 copies · chains A, C, B, D, E, F, G, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 346 | 0.68 | 0.81 | 45 | empty |
| 2 | 250 | 0.66 | 0.83 | 37 | empty |
| 3 | 251 | 0.64 | 0.82 | 33 | empty |
| 4 | 81 | 0.51 | 0.84 | 19 | empty |
| 5 | 78 | 0.50 | 0.84 | 19 | empty |
Interfaces
7 interfaces between chains.
- A–C · 879 Ų buried · 15 hydrogen bonds · protein-protein
- B–D · 821 Ų buried · 14 hydrogen bonds · protein-protein
- G–H · 767 Ų buried · 14 hydrogen bonds · protein-protein
- E–F · 755 Ų buried · 13 hydrogen bonds · protein-protein
- F–H · 554 Ų buried · 4 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 O15353
- Elsewhere: RCSB PDB 5OCN · PDBe 5OCN · UniProt O15353
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