MolNFT v1 · #80858 · protein
Structure of reduced human FBXL5 hemerythrin like domain
3U9M · F-BOX/LRR-repeat protein 5: “Structure of reduced human FBXL5 hemerythrin like domain”. X-ray diffraction, 1 ligand (FE), 4 pockets (best druggability 0.83). MolNFT v1 #80858 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 3U9M
- Type
- protein
- Length
- 628 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- F-BOX/LRR-repeat protein 5
- UniProt
- Q9UKA1
- Ligands
- FE
- Pockets
- 4 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 82% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E, G | F-BOX/LRR-repeat protein 5 | protein | 157 | 82% helix, 0% strand | Q9UKA1 |
Ligands and binding sites
- FE · Fe (III) ion · metal · 8 copies · chains A, C, E, G
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 970 | 0.83 | 0.84 | 95 | empty |
| 2 | 170 | 0.61 | 0.83 | 27 | empty |
| 3 | 77 | 0.42 | 0.80 | 19 | empty |
| 4 | 133 | 0.36 | 0.72 | 17 | empty |
Interfaces
4 interfaces between chains.
- A–C · 875 Ų buried · 11 hydrogen bonds · protein-protein
- C–G · 404 Ų buried · 4 hydrogen bonds · protein-protein
- A–G · 291 Ų buried · 5 hydrogen bonds · protein-protein
- A–E · 38 Ų buried · 0 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 Q9UKA1
- Elsewhere: RCSB PDB 3U9M · PDBe 3U9M · UniProt Q9UKA1
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