MolNFT v1 · #5192 · protein
Atomic structure of the cubic core of the pyruvate dehydrogenase multienzyme complex
1EAD · Dihydrolipoyl-transacetylase: “Atomic structure of the cubic core of the pyruvate dehydrogenase multienzyme complex”. X-ray diffraction, 1 ligand (CAO), 1 pocket (best druggability 0.64). MolNFT v1 #5192 on GenesisL1: 3D structure…
- PDB
- 1EAD
- 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
- CAO
- Pockets
- 1 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dihydrolipoyl-transacetylase (EC 2.3.1.12) | protein | 243 | 39% helix, 23% strand | P10802 |
Ligands and binding sites
- CAO · Oxidized coenzyme A · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 520 | 0.64 | 0.76 | 62 | empty |
Compared structures
- 1EAD · 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 0.98
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 1EAD · PDBe 1EAD · UniProt P10802
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.