MolNFT v2 · #158894 · protein
Horse liver alcohol dehydrogenase determined using single-particle cryo-EM at 200 keV
6NBB: “Horse liver alcohol dehydrogenase determined using single-particle cryo-EM at 200 keV”. Electron microscopy at 2.9, 2 ligands (NAD, ZN). MolNFT v2 #158894 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6NBB
- Type
- protein
- Length
- 748 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.9
- Source
- Equus caballus
- UniProt
- P00327
- Ligands
- NAD, ZN
Structure
electron microscopy · resolution 2.9 · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 374 | — | P00327 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 2 copies · chains A, B
- ZN · Zinc ion · metal · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6NBB · Horse liver alcohol dehydrogenase determined using single-particle cryo-EM at 200 kev · the same entry in another collection · chain A against A, TM-score 1.00
- P00327 · AlphaFold monomer V2.0 prediction for alcohol dehydrogenase E chain (P00327) · 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 P00327
- Elsewhere: RCSB PDB 6NBB · PDBe 6NBB · UniProt P00327
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