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Cryoem structure of arabidopsis ddr' complex (DRD1 peptide-DMS3-RDM1)

Analyse Cryoem structure of arabidopsis ddr' complex (DRD1 peptide-DMS3-RDM1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6OIT
Type
protein
Length
1,536 residues
Chains
7
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt
Q9LUJ3, Q94A79, Q9SIW2

Structure

electron microscopy · 7 distinct chains.

ChainMoleculeTypeResiduesSecondary structureUniProt
A—protein123—Q9LUJ3
B—protein125—Q9LUJ3
C—protein334—Q94A79
D—protein227—Q94A79
E—protein336—Q94A79
F—protein342—Q94A79
G—protein49—Q9SIW2

Compared structures

  • 6OIT · CryoEM structure of Arabidopsis DDR' complex (DRD1 peptide-DMS3-RDM1) · the same entry in another collection · chain F against F, TM-score 1.00
  • Q94A79 · AlphaFold monomer V2.0 prediction for protein defective in meristem silencing 3 (Q94A79) · a predicted model of the same protein · chain C against A, TM-score 0.98
  • Q9LUJ3 · AlphaFold monomer V2.0 prediction for protein RDM1 (Q9LUJ3) · a predicted model of the same protein · chain A against A, TM-score 0.92

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