Research workbench
Catalytic domain from dihydrolipoamide acetyltransferase of pyruvate dehydrogenase from escherichia COLI
Analyse Catalytic domain from dihydrolipoamide acetyltransferase of pyruvate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4N72
- Type
- protein
- Length
- 738 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pyruvate dehydrogenase (dihydrolipoyltransacetylase component)
- EC
- 2.3.1.12
- UniProt
- Q8X966
- Pockets
- 12 · best druggability 0.79
Structure
x-ray diffraction · 3 distinct chains · 38% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pyruvate dehydrogenase (dihydrolipoyltransacetylase component) (EC 2.3.1.12) | protein | 246 | 38% helix, 27% strand | Q8X966 |
| B | Pyruvate dehydrogenase (dihydrolipoyltransacetylase component) (EC 2.3.1.12) | protein | 245 | 37% helix, 27% strand | Q8X966 |
| C | Pyruvate dehydrogenase (dihydrolipoyltransacetylase component) (EC 2.3.1.12) | protein | 247 | 38% helix, 28% strand | Q8X966 |
Pockets
12 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 116 | 0.79 | 0.98 | 27 | empty |
| 2 | 728 | 0.77 | 0.82 | 65 | empty |
| 3 | 616 | 0.74 | 0.81 | 51 | empty |
| 4 | 618 | 0.74 | 0.81 | 60 | empty |
| 5 | 619 | 0.72 | 0.80 | 60 | empty |
Interfaces
3 interfaces between chains.
- B–C · 2135 Ų buried · 25 hydrogen bonds · protein-protein
- A–C · 2126 Ų buried · 26 hydrogen bonds · protein-protein
- A–B · 2117 Ų buried · 22 hydrogen bonds · protein-protein
Compared structures
- 4N72 · Catalytic domain from dihydrolipoamide acetyltransferase of pyruvate dehydrogenase from… · the same entry in another collection · chain A 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 Q8X966
- Elsewhere: RCSB PDB 4N72 · PDBe 4N72 · UniProt Q8X966
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