Research workbench
Solution structure of the lipoyl domain of the chimeric dihydrolipoyl dehydrogenase P64K from neisseria meningitidis
Analyse Solution structure of the lipoyl domain of the chimeric dihydrolipoyl… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1GJX
- Type
- protein
- Length
- 81 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pyruvate dehydrogenase
- EC
- 1.8.1.4
- UniProt
- Q9JZ09
Structure
solution nmr · 1 distinct chain · 0% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pyruvate dehydrogenase (EC 1.8.1.4) | protein | 81 | 0% helix, 28% strand | Q9JZ09 |
Compared structures
- 1GJX · Solution structure of the lipoyl domain of the chimeric dihydrolipoyl dehydrogenase P64K… · 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 Q9JZ09
- Elsewhere: RCSB PDB 1GJX · PDBe 1GJX · UniProt Q9JZ09
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