5GR8
Crystal structure of PEPR1-AtPEP1
- PDB DOI: https://doi.org/10.2210/pdb5GR8/pdb
- Classification: TRANSFERASE
- Organism(s): Arabidopsis thaliana
- Expression System: Spodoptera frugiperda
- Mutation(s): No 
- Deposited: 2016-08-08 Released: 2016-12-14 
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.59 Å
- R-Value Free: 0.288 
- R-Value Work: 0.234 
- R-Value Observed: 0.237 
This is version 2.1 of the entry. See complete history. 
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
---|---|---|---|---|---|
Molecule | Chains | Sequence Length | Organism | Details | Image |
Leucine-rich repeat receptor-like protein kinase PEPR1 | A, B [auth D] | 710 | Arabidopsis thaliana | Mutation(s): 0  Gene Names: PEPR1 EC: 2.7.11.1 | |
UniProt | |||||
Find proteins for Q9SSL9 (Arabidopsis thaliana) Explore Q9SSL9  Go to UniProtKB:  Q9SSL9 | |||||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | Q9SSL9 | ||||
Sequence AnnotationsExpand | |||||
|
Find similar proteins by: Sequence | 3D Structure
Entity ID: 2 | |||||
---|---|---|---|---|---|
Molecule | Chains | Sequence Length | Organism | Details | Image |
Elicitor peptide 1 | C [auth J], D [auth P] | 17 | Arabidopsis thaliana | Mutation(s): 0  | |
UniProt | |||||
Find proteins for Q9LV87 (Arabidopsis thaliana) Explore Q9LV87  Go to UniProtKB:  Q9LV87 | |||||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | Q9LV87 | ||||
Sequence AnnotationsExpand | |||||
|
Oligosaccharides
Small Molecules
Ligands 2 Unique | |||||
---|---|---|---|---|---|
ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
NAG Query on NAG | H [auth A] I [auth A] J [auth A] K [auth A] M [auth D] | 2-acetamido-2-deoxy-beta-D-glucopyranose C8 H15 N O6 OVRNDRQMDRJTHS-FMDGEEDCSA-N | |||
SO4 Query on SO4 | L [auth A] | SULFATE ION O4 S QAOWNCQODCNURD-UHFFFAOYSA-L |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.59 Å
- R-Value Free: 0.288 
- R-Value Work: 0.234 
- R-Value Observed: 0.237 
- Space Group: P 1 21 1
Unit Cell:
Length ( Å ) | Angle ( ˚ ) |
---|---|
a = 99.49 | α = 90 |
b = 96.967 | β = 110.79 |
c = 106.013 | γ = 90 |
Software Name | Purpose |
---|---|
PHENIX | refinement |
HKL-2000 | data reduction |
HKL-2000 | data scaling |
PHASER | phasing |
Entry History 
Deposition Data
- Released Date: 2016-12-14  Deposition Author(s): Chai, J.J., Tang, J.
Revision History (Full details and data files)
- Version 1.0: 2016-12-14
Type: Initial release - Version 2.0: 2020-07-29
Type: Remediation
Reason: Carbohydrate remediation
Changes: Atomic model, Data collection, Derived calculations, Structure summary - Version 2.1: 2023-11-08
Changes: Data collection, Database references, Refinement description, Structure summary