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UniProt O22476

Protein BRASSINOSTEROID INSENSITIVE 1 (O22476)

Protein BRASSINOSTEROID INSENSITIVE 1 (UniProt O22476), EC 2.7.10.1, 2.7.11.1: 29 experimental structures and 1 predicted model on GenesisL1, 7 ligands bound, 11 pockets. Binding sites, druggability and experiment against…

UniProt
O22476
Protein
Protein BRASSINOSTEROID INSENSITIVE 1
EC
2.7.10.1, 2.7.11.1
Experimental structures
29
Predicted models
1
Ligands
7
Pockets
11 · 5 records with a druggable one

Structures

30 records of O22476 in the MolNFT archive: 29 experimental, 1 predicted.

EntryTitleMethodChainsLigandsPockets
3RGXStructural insight into brassinosteroid perception by BRI1x-ray diffractionA——
3RGXStructural insight into brassinosteroid perception by BRI1x-ray diffractionA——
3RGZStructural insight into brassinosteroid perception by BRI1x-ray diffractionA——
3RGZStructural insight into brassinosteroid perception by BRI1x-ray diffractionA——
3RIZCrystal structure of the plant steroid receptor BRI1 ectodomainx-ray diffractionA——
3RIZCrystal structure of the plant steroid receptor BRI1 ectodomainx-ray diffractionA——
3RJ0Plant steroid receptor BRI1 ectodomain in complex with brassinolidex-ray diffractionA——
3RJ0Plant steroid receptor BRI1 ectodomain in complex with brassinolidex-ray diffractionA——
4LSACrystal structure of BRI1 sud1 (Gly643Glu) bound to brassinolidex-ray diffractionA——
4LSACrystal structure of BRI1 SUD1 (GLY643GLU) bound to brassinolidex-ray diffractionA——
4LSXPlant steroid receptor ectodomain bound to brassinolide and SERK1 co- receptor ectodomainx-ray diffractionA, B——
4M7EStructural insight into BL-induced activation of the BRI1-BAK1 complexx-ray diffractionA, B——
4M7EStructural insight into bl-induced activation of the BRI1-BAK1 complexx-ray diffractionA, B——
4OH4Crystal structure of BRI1 in complex with BKI1x-ray diffractionA, B——
4OH4Crystal structure of BRI1 in complex with BKI1x-ray diffractionA, B——
4Q5JCrystal structure of SeMet derivative BRI1 in complex with BKI1x-ray diffractionA, B——
4Q5JCrystal structure of semet derivative BRI1 in complex with BKI1x-ray diffractionA, B——
5LPBCrystal structure of the BRI1 kinase domain (865-1160) in complex with ADP from Arabidopsis thalianax-ray diffractionAADP2 (best 0.61)
5LPBCrystal structure of the BRI1 kinase domain (865-1160) in complex with ADP from arabidopsis thalianax-ray diffractionAADP—
5LPVCrystal structure of the BRI1 kinase domain (865-1160) in complex with AMPPNP and Mn from…x-ray diffractionAANP, MN2 (best 0.60)
5LPVCrystal structure of the BRI1 kinase domain (865-1160) in complex with amppnp and mn from…x-ray diffractionAANP, MN—
5LPWCrystal structure of the apo-BRI1 kinase domain (865-1160)x-ray diffractionA——
5LPWCrystal structure of the apo-BRI1 kinase domain (865-1160)x-ray diffractionA——
5LPYCrystal structure of the BRI1 kinase domain (865-1160) in complex with ATP from Arabidopsis thalianax-ray diffractionAATP2 (best 0.60)
5LPYCrystal structure of the BRI1 kinase domain (865-1160) in complex with ATP from arabidopsis thalianax-ray diffractionAATP—
5LPZCrystal structure of the BRI1 kinase domain (865-1196) in complex with ADP from Arabidopsis thalianax-ray diffractionAADP1 (best 0.61)
5LPZCrystal structure of the BRI1 kinase domain (865-1196) in complex with ADP from arabidopsis thalianax-ray diffractionAADP—
6FIFCrystal structure of the BRI1 Gly644-Asp (bri1-6) mutant from Arabidopsis thaliana.x-ray diffractionANAG, FUC, BMA4 (best 0.58)
6FIFCrystal structure of the BRI1 GLY644-asp (BRI1-6) mutant from arabidopsis thaliana.x-ray diffractionANAG, BMA—
O22476AlphaFold monomer V2.0 prediction for protein brassinosteroid insensitive 1 (O22476)predictedA——

Ligands

  • ADP · Adenosine-5'-diphosphate · in 4 records
  • ANP · Phosphoaminophosphonic acid-adenylate ester · in 2 records
  • ATP · Adenosine-5'-triphosphate · in 2 records
  • BMA · beta-D-mannopyranose · in 2 records
  • MN · Manganese (II) ion · in 2 records
  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · in 2 records
  • FUC · alpha-L-fucopyranose · in 1 record

Experiment against prediction

Elsewhere

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