MolNFT v1 · #122716 · protein

Crystal structure of the arabidopsis receptor kinase haesa lrr ectdomain (apo form).

5IXO · Receptor-like protein kinase 5: “Crystal structure of the arabidopsis receptor kinase haesa lrr ectdomain (apo form).”. X-ray diffraction, 2 ligands (NAG, MG). MolNFT v1 #122716 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 5IXO
Type: protein
Length: 596 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Receptor-like protein kinase 5
EC: 2.7.10.1, 2.7.11.1
UniProt: P47735
Ligands: NAG, MG

Structure

x-ray diffraction · 1 distinct chain · 18% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Receptor-like protein kinase 5 (EC 2.7.10.1, 2.7.11.1)	protein	596	18% helix, 26% strand	P47735

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 9 copies · chains A
MG · Magnesium ion · metal · chains A
EDO · 1,2-ethanediol · additive · 2 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Modifications

Observed in the structure: 6 glycan, 4 disulfide (N-glycosylation, disulfide).

Compared structures

5IXO · Crystal structure of the Arabidopsis receptor kinase HAESA LRR ectdomain (apo form). · the same entry in another collection · chain A against A, TM-score 1.00
P47735 · AlphaFold monomer V2.0 prediction for receptor-like protein kinase 5 (P47735) · a predicted model of the same protein · chain A against A, TM-score 0.98

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P47735
Elsewhere: RCSB PDB 5IXO · PDBe 5IXO · UniProt P47735

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