Structure of the egf-like module of human C1R, NMR, 19 structures. Determined by solution NMR. Released 17 Sept 1997.
Explore 1APQ in 3D Show helices and sheets RCSB PDB PDBe
1APQ contains 0 α-helices and 4 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 47-51 | 5 | 1 |
| β-strand | 54-58 | 5 | 1 |
| β-strand | 64-65 | 2 | 2 |
| β-strand | 72-73 | 2 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Complement protease C1R | A | protein | 53 | Homo sapiens | P00736 (AlphaFold model) |
>1APQ_1 COMPLEMENT PROTEASE C1R (chains A) AVDLDECASRSKSGEEDPQPQCQHLCHNYVGGYFCSCRPGYELQEDRHSCQAE
Solution structure of the epidermal growth factor (EGF)-like module of human complement protease C1r, an atypical member of the EGF family. Bersch, B., Hernandez, J.F., Marion, D. et al. Biochemistry (1998) 37:1204-1214. DOI 10.1021/bi971851v · PubMed
Other PDB entries of the same protein (UniProt P00736 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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