Research workbench
Peripheral-subunit binding domains from mesophilic, thermophilic, and hyperthermophilic bacteria fold by ultrafast, apparently two-state transitions
Analyse Peripheral-subunit binding domains from mesophilic, thermophilic, and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1W4K
- Type
- protein
- Length
- 51 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pyruvate dehydrogenase E2
- EC
- 2.3.1.12
- UniProt
- Q8ZUR6
Structure
solution nmr · 1 distinct chain · 45% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pyruvate dehydrogenase E2 (EC 2.3.1.12) | protein | 51 | 45% helix, 6% strand | Q8ZUR6 |
Compared structures
- 1W4K · Peripheral-subunit binding domains from mesophilic, thermophilic, and hyperthermophilic… · 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 Q8ZUR6
- Elsewhere: RCSB PDB 1W4K · PDBe 1W4K · UniProt Q8ZUR6
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