Research workbench
Crystal structure of the apo form of the E.COLI ydhf protein
Analyse Crystal structure of the apo form of the E.COLI ydhf protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1UR3
- Type
- protein
- Length
- 297 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical oxidoreductase ydhf
- EC
- 1.-.-.-
- UniProt
- P76187
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| M | Hypothetical oxidoreductase ydhf (EC 1.-.-.-) | protein | 297 | 42% helix, 15% strand | P76187 |
Ligands and binding sites
- SO4 · Sulfate ion · ion
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 124 | 0.58 | 0.84 | 24 | empty |
| 2 | 110 | 0.57 | 0.84 | 20 | empty |
| 3 | 83 | 0.34 | 0.75 | 16 | empty |
Modifications
Observed in the structure: 7 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 P76187
- Elsewhere: RCSB PDB 1UR3 · PDBe 1UR3 · UniProt P76187
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.