Research workbench
Zoogloea ramigera biosynthetic thiolase Y218E/DELH221 mutant
Analyse Zoogloea ramigera biosynthetic thiolase Y218E/DELH221 mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7LCA
- Type
- protein
- Length
- 1,549 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetyl-CoA acetyltransferase
- EC
- 2.3.1.9
- UniProt
- P07097
- Ligands
- COA, SO4, CL
- Pockets
- 18 · best druggability 0.79
Structure
x-ray diffraction · 4 distinct chains · 38% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acetyl-CoA acetyltransferase (EC 2.3.1.9) | protein | 389 | 38% helix, 23% strand | P07097 |
| B | Acetyl-CoA acetyltransferase (EC 2.3.1.9) | protein | 387 | 38% helix, 24% strand | P07097 |
| C | Acetyl-CoA acetyltransferase (EC 2.3.1.9) | protein | 387 | 37% helix, 24% strand | P07097 |
| D | Acetyl-CoA acetyltransferase (EC 2.3.1.9) | protein | 386 | 38% helix, 24% strand | P07097 |
Ligands and binding sites
- COA · Coenzyme A · ligand · 4 copies · chains A, D, B, C
- SO4 · Sulfate ion · ion · 7 copies · chains A, B, C
- CL · Chloride ion · ion · 2 copies · chains 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, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 113 | 0.79 | 0.98 | 37 | empty |
| 2 | 68 | 0.73 | 0.98 | 22 | empty |
| 3 | 265 | 0.58 | 0.78 | 44 | COA |
| 4 | 217 | 0.56 | 0.79 | 40 | COA |
| 5 | 181 | 0.55 | 0.79 | 36 | COA |
Interfaces
6 interfaces between chains.
- A–B · 2644 Ų buried · 73 hydrogen bonds · protein-protein
- C–D · 2604 Ų buried · 70 hydrogen bonds · protein-protein
- B–C · 718 Ų buried · 10 hydrogen bonds · protein-protein
- A–D · 690 Ų buried · 10 hydrogen bonds · protein-protein
- B–D · 299 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (acetylation).
Compared structures
- 7LCA · Zoogloea ramigera biosynthetic thiolase Y218E/delH221 mutant · the same entry in another collection · chain D against D, TM-score 1.00
- P07097 · AlphaFold monomer V2.0 prediction for acetyl-CoA acetyltransferase (P07097) · a predicted model of the same protein · chain C 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 P07097
- Elsewhere: RCSB PDB 7LCA · PDBe 7LCA · UniProt P07097
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