5gr8

X-ray diffraction
2.59Å resolution

Crystal structure of PEPR1-AtPEP1

Released:

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:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (3 distinct):
Leucine-rich repeat receptor-like protein kinase PEPR1 Chains: A, D
Molecule details ›
Chains: A, D
Length: 710 amino acids
Theoretical weight: 76.86 KDa
Source organism: Arabidopsis thaliana
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q9SSL9 (Residues: 29-738; Coverage: 65%)
Gene names: At1g73080, F3N23.28, PEPR1
Sequence domains:
Elicitor peptide 1 Chains: J, P
Molecule details ›
Chains: J, P
Length: 17 amino acids
Theoretical weight: 1.9 KDa
Source organism: Arabidopsis thaliana
Expression system: Not provided
UniProt:
  • Canonical: Q9LV87 (Residues: 76-92; Coverage: 19%)
Gene names: At5g64900, MXK3.13, PEP1, PROPEP1

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P21
Unit cell:
a: 99.49Å b: 96.967Å c: 106.013Å
α: 90° β: 110.79° γ: 90°
R-values:
R R work R free
0.237 0.234 0.288
Expression systems:
  • Spodoptera frugiperda
  • Not provided