Research workbench
C20S C293G mutant N-terminal human ATP citrate lyase bound to citrate
Analyse C20S C293G mutant N-terminal human ATP citrate lyase bound to citrate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5TEQ
- Type
- protein
- Length
- 1,473 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
- NA, PO4
- Pockets
- 18 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-citrate synthase (EC 2.3.3.8) | protein | 736 | 36% helix, 23% strand | P53396 |
| B | ATP-citrate synthase (EC 2.3.3.8) | protein | 737 | 36% helix, 24% strand | P53396 |
Ligands and binding sites
- NA · Sodium ion · metal · 2 copies · chains A, B
- PO4 · Phosphate ion · ion · 2 copies · chains A, B
- FLC · Citrate anion · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
18 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1053 | 0.82 | 0.83 | 127 | NA |
| 2 | 1147 | 0.82 | 0.83 | 129 | empty |
| 3 | 996 | 0.77 | 0.79 | 83 | empty |
| 4 | 251 | 0.75 | 0.89 | 44 | FLC, PO4 |
| 5 | 318 | 0.74 | 0.86 | 41 | FLC, PO4 |
Interfaces
1 interface between chains.
- A–B · 1114 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 5TEQ · C20S C293G mutant N-terminal human ATP citrate lyase bound to citrate · 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 5TEQ · PDBe 5TEQ · UniProt P53396
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