Research workbench
Crystal structure of acetyl-CoA DECARBOXYLASE/SYNTHASE complex epsilon subunit 2
Analyse Crystal structure of acetyl-CoA DECARBOXYLASE/SYNTHASE complex epsilon subunit 2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1YTL
- Type
- protein
- Length
- 631 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetyl-CoA DECARBOXYLASE/SYNTHASE complex epsilon subunit 2
- UniProt
- O30273
- Pockets
- 4 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, D | Acetyl-CoA DECARBOXYLASE/SYNTHASE complex epsilon subunit 2 | protein | 158 | 45% helix, 16% strand | O30273 |
| C | Acetyl-CoA DECARBOXYLASE/SYNTHASE complex epsilon subunit 2 | protein | 157 | 45% helix, 17% strand | O30273 |
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 | 871 | 0.76 | 0.79 | 69 | empty |
| 2 | 1050 | 0.76 | 0.78 | 80 | empty |
| 3 | 163 | 0.50 | 0.78 | 23 | empty |
| 4 | 82 | 0.43 | 0.79 | 16 | empty |
Interfaces
4 interfaces between chains.
- A–B · 552 Ų buried · 10 hydrogen bonds · protein-protein
- C–D · 468 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 220 Ų buried · 2 hydrogen bonds · protein-protein
- A–D · 193 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 1YTL · Crystal Structure of Acetyl-CoA decarboxylase/synthase complex epsilon subunit 2 · the same entry in another collection · chain D against D, TM-score 1.00
- O30273 · AlphaFold monomer V2.0 prediction for acetyl-CoA DECARBONYLASE/SYNTHASE complex subunit… · a predicted model of the same protein · chain D 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
- Every structure of UniProt O30273
- Elsewhere: RCSB PDB 1YTL · PDBe 1YTL · UniProt O30273
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