Research workbench
Cryo-electron microscopic structure of the dihydrolipoamide succinyltransferase (E2) component of the human alpha-ketoglutarate (2-oxoglutarate) dehydrogenase complex [residues 218-453]
Analyse Cryo-electron microscopic structure of the dihydrolipoamide succinyltransferase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6H05
- Type
- protein
- Length
- 236 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P36957
Structure
electron microscopy · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 236 | — | P36957 |
Compared structures
- 6H05 · Cryo-electron microscopic structure of the dihydrolipoamide succinyltransferase (E2)… · the same entry in another collection · chain A against A, TM-score 1.00
- P36957 · AlphaFold monomer V2.0 prediction for dihydrolipoyllysine-residue succinyltransferase… · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P36957
- Elsewhere: RCSB PDB 6H05 · PDBe 6H05 · UniProt P36957
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