Research workbench
Crystal structure of yfdw protein from E. COLI
Analyse Crystal structure of yfdw protein from E. COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Q7E
- Type
- protein
- Length
- 410 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical protein yfdw
- UniProt
- P69902
- Ligands
- MET
- Pockets
- 6 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hypothetical protein yfdw | protein | 410 | 40% helix, 13% strand | P69902 |
Ligands and binding sites
- MET · Methionine · ligand · 2 copies · chains A
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 7 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 135 | 0.58 | 0.83 | 21 | MPD |
| 2 | 182 | 0.55 | 0.80 | 33 | MET |
| 3 | 165 | 0.51 | 0.78 | 39 | empty |
| 4 | 124 | 0.43 | 0.76 | 15 | empty |
| 5 | 52 | 0.36 | 0.80 | 12 | MPD |
Modifications
Observed in the structure: 9 modified (engineered).
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 P69902
- Elsewhere: RCSB PDB 1Q7E · PDBe 1Q7E · UniProt P69902
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.