7brc

X-ray diffraction
2.06Å resolution

Crystal structure of the TMK3 LRR domain

Released:
Source organism: Arabidopsis thaliana
Primary publication:
Crystal structure of the extracellular domain of the receptor-like kinase TMK3 from Arabidopsis thaliana.
Acta Crystallogr F Struct Biol Commun 76 384-390 (2020)
PMID: 32744250

Function and Biology Details

Reaction catalysed:
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Receptor-like kinase TMK3 Chain: A
Molecule details ›
Chain: A
Length: 458 amino acids
Theoretical weight: 48.98 KDa
Source organism: Arabidopsis thaliana
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q9SIT1 (Residues: 25-482; Coverage: 50%)
Gene names: At2g01820, BLK2, T23K3.1, TMK3
Sequence domains: Leucine rich repeat N-terminal domain

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P21
Unit cell:
a: 49.34Å b: 115.61Å c: 57.86Å
α: 90° β: 92.349° γ: 90°
R-values:
R R work R free
0.178 0.177 0.206
Expression system: Spodoptera frugiperda