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Ternary complex crystal structure of secondary alcohol dehydrogenases from the Thermoanaerobacter ethanolicus mutants C295A and I86A provides better understanding of catalytic mechanism
Analyse Ternary complex crystal structure of secondary alcohol dehydrogenases from the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7UUT
- Type
- protein
- Length
- 1,408 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.89
- Source
- Thermoanaerobacter pseudethanolicus
- Molecule
- Secondary-alcohol dehydrogenase
- EC
- 1.1.1.80
- UniProt
- P14941
- Ligands
- NAP, 2RP, ZN, K
- Pockets
- 14 · best druggability 0.76
Structure
x-ray diffraction · resolution 1.89 · 1 distinct chain · 31% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Secondary-alcohol dehydrogenase (EC 1.1.1.80) | protein | 352 | 31% helix, 26% strand | P14941 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 4 copies · chains A, B, C, D
- 2RP · (2R)-pentan-2-ol · ligand · 4 copies · chains A, B, C, D
- ZN · Zinc ion · metal · 4 copies · chains A, B, C, D
- K · Potassium ion · metal · 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, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 847 | 0.76 | 0.80 | 85 | K |
| 2 | 830 | 0.75 | 0.80 | 66 | empty |
| 3 | 495 | 0.73 | 0.82 | 49 | NAP, 2RP |
| 4 | 474 | 0.70 | 0.80 | 49 | NAP, 2RP |
| 5 | 435 | 0.70 | 0.81 | 51 | NAP, 2RP |
Interfaces
6 interfaces between chains.
- A–B · 1901 Ų buried · 37 hydrogen bonds · protein-protein
- C–D · 1888 Ų buried · 42 hydrogen bonds · protein-protein
- A–D · 1145 Ų buried · 25 hydrogen bonds · protein-protein
- B–C · 1131 Ų buried · 21 hydrogen bonds · protein-protein
- A–C · 734 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 modified (formylation).
Compared structures
- 7UUT · Ternary complex crystal structure of secondary alcohol dehydrogenases from the… · the same entry in another collection · chain D against D, TM-score 1.00
- P14941 · AlphaFold monomer V2.0 prediction for NADP-dependent isopropanol dehydrogenase (P14941) · a predicted model of the same protein · chain C 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 P14941
- Elsewhere: RCSB PDB 7UUT · PDBe 7UUT · UniProt P14941
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