Research workbench
Refined NMR structure of the FHA1 domain of yeast RAD53
Analyse Refined NMR structure of the FHA1 domain of yeast RAD53 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1K3J
- Type
- protein
- Length
- 151 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein kinase SPK1
- EC
- 2.7.1.-
- UniProt
- P22216
Structure
solution nmr · 1 distinct chain · 16% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein kinase SPK1 (EC 2.7.1.-) | protein | 151 | 16% helix, 31% strand | P22216 |
Compared structures
- 1K3J · Refined NMR Structure of the FHA1 Domain of Yeast Rad53 · the same entry in another collection · chain A against A, TM-score 1.00
- P22216 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase RAD53 (P22216) · a predicted model of the same protein · chain A against A, TM-score 0.83
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 P22216
- Elsewhere: RCSB PDB 1K3J · PDBe 1K3J · UniProt P22216
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.