MolNFT v1 · #151770 · protein
Structure of the citryl-CoA lyase core module of human ATP citrate lyase in complex with citrate and coash in space group C2221
6HXM · ATP-citrate synthase: “Structure of the citryl-CoA lyase core module of human ATP citrate lyase in complex with citrate and coash in…”. X-ray diffraction, 1 ligand (COA), 4 pockets (best druggability 0.63). MolNFT v1 #151770 on…
- PDB
- 6HXM
- Type
- protein
- Length
- 528 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
- COA
- Pockets
- 4 · best druggability 0.63
Structure
x-ray diffraction · 2 distinct chains · 58% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-citrate synthase (EC 2.3.3.8) | protein | 263 | 59% helix, 5% strand | P53396 |
| B | ATP-citrate synthase (EC 2.3.3.8) | protein | 265 | 57% helix, 4% strand | P53396 |
Ligands and binding sites
- COA · Coenzyme A · ligand · 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
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 401 | 0.63 | 0.77 | 44 | COA, FLC |
| 2 | 297 | 0.59 | 0.78 | 35 | COA, FLC |
| 3 | 269 | 0.53 | 0.75 | 37 | empty |
| 4 | 52 | 0.30 | 0.76 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 3519 Ų buried · 33 hydrogen bonds · protein-protein
Compared structures
- 6HXM · Structure of the citryl-CoA lyase core module of human ATP citrate lyase in complex with… · 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 B 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 6HXM · PDBe 6HXM · UniProt P53396
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