Research workbench
1.8 ångström structure of xylose reductase from candida tenuis in complex with NAD
Analyse 1.8 ångström structure of xylose reductase from candida tenuis in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1MI3
- Type
- protein
- Length
- 1,276 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Xylose reductase
- EC
- 1.1.1.21
- UniProt
- O74237
- Ligands
- NAD
- Pockets
- 14 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Xylose reductase (EC 1.1.1.21) | protein | 319 | 40% helix, 15% strand | O74237 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 327 | 0.72 | 0.84 | 44 | NAD |
| 2 | 316 | 0.72 | 0.85 | 42 | NAD |
| 3 | 306 | 0.71 | 0.85 | 44 | NAD |
| 4 | 295 | 0.69 | 0.83 | 42 | NAD |
| 5 | 447 | 0.64 | 0.77 | 40 | empty |
Interfaces
3 interfaces between chains.
- C–D · 1312 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 1293 Ų buried · 10 hydrogen bonds · protein-protein
- B–D · 121 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 1MI3 · 1.8 Angstrom structure of xylose reductase from Candida tenuis in complex with NAD · the same entry in another collection · chain A against A, TM-score 1.00
- O74237 · AlphaFold monomer V2.0 prediction for NAD(P)H-dependent D-xylose reductase (O74237) · a predicted model of the same protein · 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 O74237
- Elsewhere: RCSB PDB 1MI3 · PDBe 1MI3 · UniProt O74237
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.