Research workbench
Crystal structure of human alcohol dehydrogenase beta-1-beta-1 isoform complexed with N-benzylformamide determined to 1.6 ångström resolution
Analyse Crystal structure of human alcohol dehydrogenase beta-1-beta-1 isoform… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1U3U
- Type
- protein
- Length
- 748 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alcohol dehydrogenase beta chain
- EC
- 1.1.1.1
- UniProt
- P00325
- Ligands
- NAD, BNF, ZN, PO4
- Pockets
- 3 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Alcohol dehydrogenase beta chain (EC 1.1.1.1) | protein | 374 | 30% helix, 26% strand | P00325 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 2 copies · chains A, B
- BNF · N-benzylformamide · ligand · 2 copies · chains A, B
- ZN · Zinc ion · metal · 4 copies · chains A, B
- PO4 · Phosphate ion · ion · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 483 | 0.76 | 0.84 | 60 | NAD, BNF |
| 2 | 532 | 0.76 | 0.83 | 65 | NAD, BNF |
| 3 | 525 | 0.68 | 0.78 | 61 | empty |
Interfaces
1 interface between chains.
- A–B · 1738 Ų buried · 30 hydrogen bonds · protein-protein
Compared structures
- 1U3U · Crystal Structure of Human Alcohol Dehydrogenase Beta-1-Beta-1 Isoform Complexed with… · the same entry in another collection · chain A against A, TM-score 1.00
- P00325 · AlphaFold monomer V2.0 prediction for all-trans-retinol dehydrogenase [NAD(+)] ADH1B… · a predicted model of the same protein · chain B 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 P00325
- Elsewhere: RCSB PDB 1U3U · PDBe 1U3U · UniProt P00325
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.