MolNFT v1 · #13400 · protein
Three-dimensional structure of the lipoyl domain from bacillus stearothermophilus pyruvate dehydrogenase multienzyme complex
1LAB · Dihydrolipoamide acetyltransferase: “Three-dimensional structure of the lipoyl domain from bacillus stearothermophilus pyruvate dehydrogenase…”. Solution nmr, 1 pocket (best druggability 0.59). MolNFT v1 #13400 on GenesisL1: 3D…
- PDB
- 1LAB
- Type
- protein
- Length
- 80 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dihydrolipoamide acetyltransferase
- EC
- 2.3.1.12
- UniProt
- P11961
- Pockets
- 1 · best druggability 0.59
Structure
solution nmr · 1 distinct chain · 0% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dihydrolipoamide acetyltransferase (EC 2.3.1.12) | protein | 80 | 0% helix, 30% strand | P11961 |
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 | 168 | 0.59 | 0.82 | 29 | empty |
Compared structures
- 1LAB · Three-dimensional structure of the lipoyl domain from bacillus stearothermophilus… · the same entry in another collection · chain A against A, TM-score 1.00
- P11961 · AlphaFold monomer V2.0 prediction for dihydrolipoyllysine-residue acetyltransferase… · a predicted model of the same protein · chain A against A, TM-score 0.71
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 P11961
- Elsewhere: RCSB PDB 1LAB · PDBe 1LAB · UniProt P11961
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