Research workbench
Crystal structure of citrate synthase from homo sapiens
Analyse Crystal structure of citrate synthase from homo sapiens in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5UZQ
- Type
- protein
- Length
- 434 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Citrate synthase
- UniProt
- B4DJV2
- Pockets
- 3 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 64% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Citrate synthase | protein | 434 | 64% helix, 4% strand | B4DJV2 |
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 | 215 | 0.52 | 0.77 | 28 | empty |
| 2 | 182 | 0.44 | 0.74 | 30 | empty |
| 3 | 85 | 0.34 | 0.74 | 16 | empty |
Modifications
Observed in the structure: 2 modified (artifact).
Compared structures
- 5UZQ · Crystal structure of citrate synthase from homo sapiens · the same entry in another collection · 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 B4DJV2
- Elsewhere: RCSB PDB 5UZQ · PDBe 5UZQ · UniProt B4DJV2
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