Research workbench
Crystal structure of alcohol dehydrogenase zinc-binding domain protein from burkholderia ambifaria
Analyse Crystal structure of alcohol dehydrogenase zinc-binding domain protein from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5TNX
- Type
- protein
- Length
- 370 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alcohol dehydrogenase zinc-binding domain protein
- UniProt
- B1Z4S6
- Ligands
- ZN
- Pockets
- 3 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alcohol dehydrogenase zinc-binding domain protein | protein | 370 | 33% helix, 27% strand | B1Z4S6 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
- EDO · 1,2-ethanediol · additive · 5 copies · chains A
- CIT · Citric acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 596 | 0.69 | 0.78 | 59 | CIT, EDO |
| 2 | 119 | 0.48 | 0.79 | 23 | empty |
| 3 | 95 | 0.40 | 0.77 | 19 | empty |
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 B1Z4S6
- Elsewhere: RCSB PDB 5TNX · PDBe 5TNX · UniProt B1Z4S6
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