Research workbench
Crystal structure of rat biliverdin reductase at 1.4 a
Analyse Crystal structure of rat biliverdin reductase at 1.4 a in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1GCU
- Type
- protein
- Length
- 292 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Biliverdin reductase a
- EC
- 1.3.1.24
- UniProt
- P46844
- Pockets
- 4 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Biliverdin reductase a (EC 1.3.1.24) | protein | 292 | 41% helix, 27% strand | P46844 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 661 | 0.68 | 0.76 | 58 | empty |
| 2 | 96 | 0.43 | 0.78 | 16 | empty |
| 3 | 104 | 0.42 | 0.77 | 15 | empty |
| 4 | 92 | 0.40 | 0.77 | 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 P46844
- Elsewhere: RCSB PDB 1GCU · PDBe 1GCU · UniProt P46844
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.