Research workbench
Innermost lipoyl domain of the pyruvate dehydrogenase from escherichia COLI
Analyse Innermost lipoyl domain of the pyruvate dehydrogenase from escherichia COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QJO
- Type
- protein
- Length
- 80 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dihydrolipoamide acetyltransferase
- UniProt
- P06959
Structure
solution nmr · 1 distinct chain · 0% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dihydrolipoamide acetyltransferase | protein | 80 | 0% helix, 43% strand | P06959 |
Compared structures
- 1QJO · Innermost lipoyl domain of the pyruvate dehydrogenase from escherichia COLI · the same entry in another collection · chain A against A, TM-score 1.00
- P06959 · AlphaFold monomer V2.0 prediction for dihydrolipoyllysine-residue acetyltransferase… · a predicted model of the same protein · chain A against A, TM-score 0.84
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 P06959
- Elsewhere: RCSB PDB 1QJO · PDBe 1QJO · UniProt P06959
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