Structure of PDB 5lpv Chain A

Receptor sequence
>5lpvA (length=285) Species: 3702 (Arabidopsis thaliana) [Search protein sequence]
PLRKLAFADLLQATNGFHNDSLIGSGGFGDVYKAILKDGSAVAIKKLIHV
SGQGDREFMAEMETIGKIKHRNLVPLLGYCKVGDERLLVYEFMKYGSLED
VLHDGVKLNWSTRRKIAIGSARGLAFLHHNCSPHIIHRDMKSSNVLLDEN
LEARVSDFGMARLMSAMDTHLSVSTLAGTPGYVPPEYYQSFRCSTKGDVY
SYGVVLLELLTGKRPTDSPNLVGWVKQHAKLRISDVFDPELMKEDPALEI
ELLQHLKVAVACLDDRAWRRPTMVQVMAMFKEIQA
3D structure
PDB5lpv Crystal structures of the phosphorylated BRI1 kinase domain and implications for brassinosteroid signal initiation.
ChainA
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D1009 K1011 S1013 N1014 D1027 M1037 T1049
Catalytic site (residue number reindexed from 1) D139 K141 S143 N144 D157 M167 T179
Enzyme Commision number 2.7.10.1: receptor protein-tyrosine kinase.
2.7.11.1: non-specific serine/threonine protein kinase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ANP A F894 V897 A909 K911 M959 K1011 L1016 D1027 F28 V31 A43 K45 M93 K141 L146 D157
BS02 MN A N1014 D1027 N144 D157
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5lpv, PDBe:5lpv, PDBj:5lpv
PDBsum5lpv
PubMed
UniProtO22476|BRI1_ARATH Protein BRASSINOSTEROID INSENSITIVE 1 (Gene Name=BRI1)

[Back to BioLiP]