MolNFT v1 · #60510 · protein
Crystallographic refinement and atomic models of two different forms of citrate synthase at 2.7 and 1.7 ångströms resolution
3CTS: “Crystallographic refinement and atomic models of two different forms of citrate synthase at 2.7 and 1.7…”. X-ray diffraction, 1 ligand (COA), 2 pockets (best druggability 0.68). MolNFT v1 #60510 on GenesisL1: 3D structure, binding…
- 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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