3uim

X-ray diffraction
2.2Å resolution

Structural basis for the impact of phosphorylation on plant receptor-like kinase BAK1 activation

Released:

Function and Biology Details

Reactions catalysed:
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-188228 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
BRASSINOSTEROID INSENSITIVE 1-associated receptor kinase 1 Chain: A
Molecule details ›
Chain: A
Length: 326 amino acids
Theoretical weight: 37.52 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
  • Canonical: Q94F62 (Residues: 258-583; Coverage: 55%)
Gene names: At4g33430, BAK1, ELG, F17M5.190, SERK3
Sequence domains: Protein tyrosine and serine/threonine kinase
Structure domains:

Ligands and Environments

1 bound ligand:
2 modified residues:

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: C2
Unit cell:
a: 70.11Å b: 74.7Å c: 71.924Å
α: 90° β: 93.72° γ: 90°
R-values:
R R work R free
0.237 0.234 0.277
Expression system: Escherichia coli