MolNFT v1 · #157701 · protein
Crystal structure of an alcohol dehydrogenase from elizabethkingia anophelis NUHP1
6N7L: “Crystal structure of an alcohol dehydrogenase from elizabethkingia anophelis NUHP1”. X-ray diffraction, 3 ligands (NAD, ZN, CL). MolNFT v1 #157701 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6N7L
- Type
- protein
- Length
- 4,102 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A077EGR8
- Ligands
- NAD, ZN, CL
Structure
x-ray diffraction · 6 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, H, K | — | protein | 342 | — | A0A077EGR8 |
| C | — | protein | 344 | — | A0A077EGR8 |
| D, J | — | protein | 343 | — | A0A077EGR8 |
| E, G, L | — | protein | 340 | — | A0A077EGR8 |
| F | — | protein | 343 | — | A0A077EGR8 |
| I | — | protein | 341 | — | A0A077EGR8 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 12 copies · chains A, D, B, C, E, H, F, G, I, L, J, K
- ZN · Zinc ion · metal · 24 copies · chains A, B, C, D, E, F, G, H, I, J, K, L
- CL · Chloride ion · ion · 12 copies · chains A, B, C, D, E, F, G, H, I, J, K, L
- EDO · 1,2-ethanediol · additive · 90 copies · chains A, C, D, B, J, G, F, E, H, I, K, L
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6N7L · Crystal structure of an alcohol dehydrogenase from Elizabethkingia anophelis NUHP1 · the same entry in another collection · 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 A0A077EGR8
- Elsewhere: RCSB PDB 6N7L · PDBe 6N7L · UniProt A0A077EGR8
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.