MolNFT v1 · #12734 · protein
Crystal structure of a glycerol dehydrogenase (TM0423) from thermotoga maritima at 1.5 a resolution
1KQ3: “Crystal structure of a glycerol dehydrogenase (TM0423) from thermotoga maritima at 1.5 a resolution”. X-ray diffraction, 2 ligands (ZN, CL), 2 pockets (best druggability 0.71). MolNFT v1 #12734 on GenesisL1: 3D structure, binding…
- PDB
- 1KQ3
- Type
- protein
- Length
- 364 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glycerol dehydrogenase
- UniProt
- Q9WYQ4
- Ligands
- ZN, CL
- Pockets
- 2 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 54% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycerol dehydrogenase | protein | 364 | 54% helix, 13% strand | Q9WYQ4 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
- CL · Chloride ion · ion · chains A
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 611 | 0.71 | 0.79 | 61 | TRS |
| 2 | 53 | 0.40 | 0.81 | 13 | empty |
Compared structures
- 1KQ3 · Crystal structure of a glycerol dehydrogenase (TM0423) from thermotoga maritima at 1.5 a… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9WYQ4 · AlphaFold monomer V2.0 prediction for glycerol dehydrogenase (Q9WYQ4) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q9WYQ4
- Elsewhere: RCSB PDB 1KQ3 · PDBe 1KQ3 · UniProt Q9WYQ4
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