Research workbench
E. COLI pyruvate dehydrogenase complex E1 E235A mutant with low tdp concentration
Analyse E. COLI pyruvate dehydrogenase complex E1 E235A mutant with low tdp… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3LQ2
- Type
- protein
- Length
- 1,602 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0AFG9
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 801 | — | P0AFG9 |
Compared structures
- 3LQ2 · E. coli pyruvate dehydrogenase complex E1 E235A mutant with low TDP concentration · the same entry in another collection · chain A against A, TM-score 1.00
- P0AFG9 · AlphaFold monomer V2.0 prediction for pyruvate dehydrogenase E1 component (P0AFG9) · a predicted model of the same protein · 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 P0AFG9
- Elsewhere: RCSB PDB 3LQ2 · PDBe 3LQ2 · UniProt P0AFG9
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