Research workbench
Structure of ternary complexes of citrate synthase with D-and L- malate: mechanistic implications
Analyse Structure of ternary complexes of citrate synthase with D-and L- malate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4CSC
- Type
- protein
- Length
- 429 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Citrate synthase
- EC
- 4.1.3.7
- UniProt
- P23007
- Ligands
- MLT, ACO
- Pockets
- 3 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 62% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Citrate synthase (EC 4.1.3.7) | protein | 429 | 62% helix, 2% strand | P23007 |
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 | 462 | 0.65 | 0.77 | 53 | MLT, ACO |
| 2 | 164 | 0.45 | 0.75 | 33 | empty |
| 3 | 89 | 0.42 | 0.79 | 17 | empty |
Compared structures
- 4CSC · Structure of ternary complexes of citrate synthase with D-and L-malate: mechanistic… · 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 P23007
- Elsewhere: RCSB PDB 4CSC · PDBe 4CSC · UniProt P23007
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