1APQ: Egf-like module of human C1R, NMR, 19 structures

Structure of the egf-like module of human C1R, NMR, 19 structures. Determined by solution NMR. Released 17 Sept 1997.

Method
Solution NMR
Organism
Homo sapiens
Chains
1
Atoms
415
Mol. weight
5.98 kDa
Released
17 Sept 1997

Explore 1APQ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 0 helices, 4 β-strands

ElementResiduesLengthSheet
β-strand47-5151
β-strand54-5851
β-strand64-6522
β-strand72-7322

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Complement protease C1RAprotein53Homo sapiensP00736 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1APQ_1 COMPLEMENT PROTEASE C1R (chains A)
AVDLDECASRSKSGEEDPQPQCQHLCHNYVGGYFCSCRPGYELQEDRHSCQAE

Primary citation

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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