Research workbench
An inhibited conformation for the protein kinase domain of the saccharomyces cerevisiae ampk homolog SNF1
Analyse An inhibited conformation for the protein kinase domain of the saccharomyces… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3MN3
- Type
- protein
- Length
- 252 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P06782
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 252 | — | P06782 |
Compared structures
- 3MN3 · An inhibited conformation for the protein kinase domain of the Saccharomyces cerevisiae… · the same entry in another collection · chain A against A, TM-score 1.00
- P06782 · AlphaFold monomer V2.0 prediction for carbon catabolite-derepressing protein kinase… · a predicted model of the same protein · chain A against A, TM-score 0.86
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 P06782
- Elsewhere: RCSB PDB 3MN3 · PDBe 3MN3 · UniProt P06782
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