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Structure of the EGF-like module of human C1R, NMR, 19 structures

Analyse Structure of the EGF-like module of human C1R, NMR, 19 structures in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1APQ
Type
protein
Length
53 residues
Chains
1
Method
solution nmr
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
NOT
Source
Homo sapiens
Molecule
Complement protease C1R
EC
3.4.21.41
UniProt
P00736

Structure

solution nmr · resolution NOT · 1 distinct chain · 0% helix, 26% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AComplement protease C1R (EC 3.4.21.41)protein530% helix, 26% strandP00736

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

  • 1APQ · Structure of the EGF-like module of human C1R, NMR, 19 structures · 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 0.68

Analyse

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