Research workbench
Crystallographic refinement and atomic models of two different forms of citrate synthase at 2.7 and 1.7 ångströms resolution
Analyse Crystallographic refinement and atomic models of two different forms of citrate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3CTS
- 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
- Ligands
- COA
- Pockets
- 2 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 62% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Citrate synthase (EC 4.1.3.7) | protein | 429 | 62% helix, 3% strand | — |
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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 674 | 0.68 | 0.76 | 77 | COA, CIT |
| 2 | 89 | 0.41 | 0.78 | 17 | empty |
Compared structures
- 3CTS · Crystallographic refinement and atomic models of two different forms of citrate synthase… · 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
- Elsewhere: RCSB PDB 3CTS · PDBe 3CTS
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