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Active dimeric structure of the catalytic domain of C1R reveals enzyme-product like contacts

Analyse Active dimeric structure of the catalytic domain of C1R reveals enzyme-product… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2QY0
Type
protein
Length
780 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt
P00736

Structure

x-ray diffraction · 4 distinct chains.

ChainMoleculeTypeResiduesSecondary structureUniProt
A—protein154—P00736
B—protein236—P00736
C—protein153—P00736
D—protein237—P00736

Compared structures

  • 2QY0 · Active dimeric structure of the catalytic domain of C1r reveals enzyme-product like… · the same entry in another collection · chain D against D, TM-score 1.00
  • P00736 · AlphaFold monomer V2.0 prediction for complement C1R subcomponent (P00736) · a predicted model of the same protein · chain B against A, TM-score 0.98

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