Research workbench
C20S, C293G mutant N-terminal human ATP citrate lyase bound to 4R- hydroxycitrate
Analyse C20S, C293G mutant N-terminal human ATP citrate lyase bound to 4R… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5TE1
- Type
- protein
- Length
- 1,485 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-citrate synthase
- EC
- 2.3.3.8
- UniProt
- P53396
- Ligands
- 7A2, NA, PO4
- Pockets
- 17 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-citrate synthase (EC 2.3.3.8) | protein | 742 | 37% helix, 24% strand | P53396 |
| B | ATP-citrate synthase (EC 2.3.3.8) | protein | 743 | 37% helix, 24% strand | P53396 |
Ligands and binding sites
- 7A2 · 3-C-carboxy-2-deoxy-L-threo-pentaric acid · ligand · 2 copies · chains A, B
- NA · Sodium ion · metal · 2 copies · chains A, B
- PO4 · Phosphate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
17 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1154 | 0.84 | 0.85 | 130 | 7A2, PO4 |
| 2 | 1170 | 0.83 | 0.84 | 125 | 7A2, PO4, NA |
| 3 | 902 | 0.77 | 0.80 | 98 | empty |
| 4 | 229 | 0.57 | 0.79 | 34 | empty |
| 5 | 187 | 0.55 | 0.79 | 29 | empty |
Interfaces
1 interface between chains.
- A–B · 1149 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 5TE1 · C20S, C293G Mutant N-terminal Human ATP Citrate Lyase Bound to 4R-Hydroxycitrate · the same entry in another collection · chain A against A, TM-score 1.00
- P53396 · AlphaFold monomer V2.0 prediction for ATP-citrate synthase (P53396) · 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 P53396
- Elsewhere: RCSB PDB 5TE1 · PDBe 5TE1 · UniProt P53396
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