MolNFT v1 · #69254 · protein
Crystal structure of the Q5LES9_BACFN protein from bacteroides fragilis. northeast structural genomics consortium target BFR250.
3KKZ · Uncharacterized protein Q5LES9: “Crystal structure of the Q5LES9_BACFN protein from bacteroides fragilis. northeast structural genomics…”. X-ray diffraction, 1 ligand (SAM), 5 pockets (best druggability 0.69). MolNFT v1 #69254 on…
- PDB
- 3KKZ
- Type
- protein
- Length
- 506 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized protein Q5LES9
- UniProt
- Q5LES9
- Ligands
- SAM
- Pockets
- 5 · best druggability 0.69
Structure
x-ray diffraction · 2 distinct chains · 46% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized protein Q5LES9 | protein | 256 | 47% helix, 22% strand | Q5LES9 |
| B | Uncharacterized protein Q5LES9 | protein | 250 | 46% helix, 22% strand | Q5LES9 |
Ligands and binding sites
- SAM · S-adenosylmethionine · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 472 | 0.69 | 0.79 | 45 | SAM |
| 2 | 453 | 0.69 | 0.80 | 42 | SAM |
| 3 | 239 | 0.55 | 0.77 | 33 | empty |
| 4 | 218 | 0.53 | 0.77 | 30 | empty |
| 5 | 64 | 0.32 | 0.75 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1016 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 modified (engineered).
Compared structures
- 3KKZ · Crystal structure of the Q5LES9_BACFN protein from Bacteroides fragilis. Northeast… · the same entry in another collection · chain A against A, TM-score 1.00
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 Q5LES9
- Elsewhere: RCSB PDB 3KKZ · PDBe 3KKZ · UniProt Q5LES9
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