MolNFT v1 · #19323 · protein
Human glyoxalase II with cacodylate and acetate ions present in the active site
1QH3 · Protein (hydroxyacylglutathione hydrolase): “Human glyoxalase II with cacodylate and acetate ions present in the active site”. X-ray diffraction, 3 ligands (ZN, MN, CL), 3 pockets (best druggability 0.60). MolNFT v1 #19323 on…
- PDB
- 1QH3
- Type
- protein
- Length
- 520 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (hydroxyacylglutathione hydrolase)
- EC
- 3.1.2.6
- UniProt
- Q16775
- Ligands
- ZN, MN, CL
- Pockets
- 3 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Protein (hydroxyacylglutathione hydrolase) (EC 3.1.2.6) | protein | 260 | 33% helix, 25% strand | Q16775 |
Ligands and binding sites
- ZN · Zinc ion · metal · 4 copies · chains A, B
- MN · Manganese (II) ion · metal · 2 copies · chains A, B
- CL · Chloride ion · ion · chains A, B
- CAC · Cacodylate ion · additive · 4 copies · chains A, B
- ACT · Acetate ion · additive · 2 copies · chains A, B
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 | 302 | 0.60 | 0.78 | 26 | CL |
| 2 | 110 | 0.38 | 0.74 | 22 | CAC, ACT |
| 3 | 95 | 0.37 | 0.75 | 19 | CAC, ACT |
Interfaces
1 interface between chains.
- A–B · 331 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 1QH3 · Human glyoxalase II with cacodylate and acetate ions present in the active site · the same entry in another collection · chain A against A, TM-score 1.00
- Q16775 · AlphaFold monomer V2.0 prediction for hydroxyacylglutathione hydrolase, mitochondrial… · a predicted model of the same protein · 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 Q16775
- Elsewhere: RCSB PDB 1QH3 · PDBe 1QH3 · UniProt Q16775
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