Research workbench
Atomic structure of the cubic core of the pyruvate dehydrogenase multienzyme complex
Analyse Atomic structure of the cubic core of the pyruvate dehydrogenase multienzyme… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1EAB
- Type
- protein
- Length
- 243 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dihydrolipoyl-transacetylase
- EC
- 2.3.1.12
- UniProt
- P10802
- Ligands
- COA, LPM
- Pockets
- 3 · best druggability 0.54
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dihydrolipoyl-transacetylase (EC 2.3.1.12) | protein | 243 | 40% helix, 23% strand | P10802 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 239 | 0.54 | 0.77 | 36 | empty |
| 2 | 247 | 0.53 | 0.76 | 31 | empty |
| 3 | 61 | 0.32 | 0.75 | 15 | empty |
Compared structures
- 1EAB · Atomic structure of the cubic core of the pyruvate dehydrogenase multienzyme complex · the same entry in another collection · chain A against A, TM-score 1.00
- P10802 · AlphaFold monomer V2.0 prediction for dihydrolipoyllysine-residue acetyltransferase… · 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 P10802
- Elsewhere: RCSB PDB 1EAB · PDBe 1EAB · UniProt P10802
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