Research workbench
Urocanate reductase in complex with imidazole propionate
Analyse Urocanate reductase in complex with imidazole propionate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6T88
- Type
- protein
- Length
- 454 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Urocanate reductase
- EC
- 1.3.99.33
- UniProt
- Q8CVD0
- Ligands
- FAD, MWQ, NA, CL
- Pockets
- 2 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Urocanate reductase (EC 1.3.99.33) | protein | 454 | 37% helix, 24% strand | Q8CVD0 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains A
- MWQ · 3-(1~{H}-imidazol-5-yl)propanoic acid · ligand · chains A
- NA · Sodium ion · metal · chains A
- CL · Chloride ion · ion · 3 copies · chains A
- GOL · Glycerol · additive · 8 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 562 | 0.81 | 0.87 | 97 | FAD, MWQ, CL, GOL |
| 2 | 79 | 0.34 | 0.75 | 17 | empty |
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 Q8CVD0
- Elsewhere: RCSB PDB 6T88 · PDBe 6T88 · UniProt Q8CVD0
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