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Crystal structure of homocitrate synthase from Thermus thermophilus complexed with magnesuim ion and alpha-ketoglutarate
Analyse Crystal structure of homocitrate synthase from Thermus thermophilus complexed… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ZYF
- Type
- protein
- Length
- 314 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.15
- Source
- Thermus thermophilus
- Molecule
- Homocitrate synthase
- EC
- 2.3.3.14
- UniProt
- O87198
- Ligands
- AKG, MG
- Pockets
- 2 · best druggability 0.50
Structure
x-ray diffraction · resolution 2.15 · 1 distinct chain · 47% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Homocitrate synthase (EC 2.3.3.14) | protein | 314 | 47% helix, 17% strand | O87198 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 163 | 0.50 | 0.78 | 33 | AKG, MG |
| 2 | 76 | 0.33 | 0.75 | 18 | empty |
Compared structures
- 2ZYF · Crystal structure of homocitrate synthase from thermus thermophilus complexed with… · the same entry in another collection · chain A against A, TM-score 1.00
- O87198 · AlphaFold monomer V2.0 prediction for homocitrate synthase (O87198) · a predicted model of the same protein · chain A 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 O87198
- Elsewhere: RCSB PDB 2ZYF · PDBe 2ZYF · UniProt O87198
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