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Monomeric structure of the zymogen of complement protease C1R

Analyse Monomeric structure of the zymogen of complement protease C1R in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1MD7
Type
protein
Length
304 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
C1R complement serine protease
EC
3.4.21.41
UniProt
P00736
Ligands
NAG
Pockets
3 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 10% helix, 30% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AC1R complement serine protease (EC 3.4.21.41)protein30410% helix, 30% strandP00736

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A

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

Pockets

3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13260.610.7839empty
21740.450.7421empty
3560.320.7613empty

Modifications

Observed in the structure: 5 disulfide, 1 glycan (disulfide, N-glycosylation).

Compared structures

  • 1MD7 · Monomeric structure of the zymogen of complement protease C1r · the same entry in another collection · chain A against A, TM-score 1.00
  • P00736 · AlphaFold monomer V2.0 prediction for complement C1R subcomponent (P00736) · a predicted model of the same protein · chain A against A, TM-score 0.91

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