Research workbench
Crystal structure of homocitrate synthase from thermus thermophilus complexed with homocitrate
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
- 2ZTK
- Type
- protein
- Length
- 312 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Homocitrate synthase
- EC
- 2.3.3.14
- UniProt
- O87198
- Ligands
- HCA, CU
- Pockets
- 3 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Homocitrate synthase (EC 2.3.3.14) | protein | 312 | 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
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 | 127 | 0.51 | 0.80 | 16 | empty |
| 2 | 75 | 0.41 | 0.80 | 21 | HCA |
| 3 | 87 | 0.35 | 0.75 | 18 | empty |
Compared structures
- 2ZTK · 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 2ZTK · PDBe 2ZTK · UniProt O87198
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