Research workbench
Contribution of PRO275 to the thermostability of the alcohol dehydrogenases (adhs)
Analyse Contribution of PRO275 to the thermostability of the alcohol dehydrogenases… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2NVB
- Type
- protein
- Length
- 1,408 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- NADP-dependent alcohol dehydrogenase
- EC
- 1.1.1.2
- UniProt
- P14941
- Ligands
- NAP, ZN
- Pockets
- 13 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | NADP-dependent alcohol dehydrogenase (EC 1.1.1.2) | protein | 352 | 32% helix, 26% strand | P14941 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 4 copies · chains A, B, C, D
- ZN · Zinc 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
13 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 542 | 0.75 | 0.82 | 63 | empty |
| 2 | 556 | 0.74 | 0.81 | 64 | empty |
| 3 | 486 | 0.72 | 0.81 | 55 | NAP |
| 4 | 394 | 0.70 | 0.82 | 51 | NAP |
| 5 | 442 | 0.70 | 0.81 | 53 | ZN, NAP |
Interfaces
6 interfaces between chains.
- A–B · 1958 Ų buried · 40 hydrogen bonds · protein-protein
- C–D · 1930 Ų buried · 44 hydrogen bonds · protein-protein
- A–D · 1169 Ų buried · 26 hydrogen bonds · protein-protein
- B–C · 1164 Ų buried · 26 hydrogen bonds · protein-protein
- B–D · 753 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 2NVB · Contribution of Pro275 to the Thermostability of the Alcohol Dehydrogenases (ADHs) · 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 2NVB · PDBe 2NVB · UniProt P14941
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