Research workbench
Crystal structure of mouse glyoxalase I complexed with zopolrestat
Analyse Crystal structure of mouse glyoxalase I complexed with zopolrestat in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4KYH
- Type
- protein
- Length
- 353 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lactoylglutathione lyase
- EC
- 4.4.1.5
- UniProt
- Q9CPU0
- Ligands
- ZST, ZN
- Pockets
- 4 · best druggability 0.62
Structure
x-ray diffraction · 2 distinct chains · 27% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lactoylglutathione lyase (EC 4.4.1.5) | protein | 177 | 27% helix, 28% strand | Q9CPU0 |
| B | Lactoylglutathione lyase (EC 4.4.1.5) | protein | 176 | 28% helix, 28% strand | Q9CPU0 |
Ligands and binding sites
- ZST · 3,4-dihydro-4-oxo-3-((5-trifluoromethyl-2-benzothiazolyl)methyl)-1-phthalazine acetic acid · ligand · chains A, B
- ZN · Zinc ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 242 | 0.62 | 0.80 | 28 | ZST |
| 2 | 316 | 0.61 | 0.78 | 30 | empty |
| 3 | 154 | 0.42 | 0.74 | 27 | empty |
| 4 | 63 | 0.31 | 0.75 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 3721 Ų buried · 48 hydrogen bonds · protein-protein
Compared structures
- 4KYH · Crystal structure of mouse glyoxalase I complexed with zopolrestat · the same entry in another collection · chain A against A, TM-score 1.00
- Q9CPU0 · AlphaFold monomer V2.0 prediction for lactoylglutathione lyase (Q9CPU0) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 Q9CPU0
- Elsewhere: RCSB PDB 4KYH · PDBe 4KYH · UniProt Q9CPU0
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