6JEC: Triple-helix region of human collagen type II

Structure of a triple-helix region of human collagen type II. Determined by X-ray diffraction at 2.05 Å resolution. Released 5 Feb 2020.

Method: X-ray diffraction
Resolution: 2.05 Å
Organism: Homo sapiens
Chains: 3
Atoms: 700
Mol. weight: 8.22 kDa
Released: 5 Feb 2020

Explore 6JEC in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6JEC contains 8 α-helices and 0 β-strands across 3 chains. 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: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	2-20	19
α-helix	22-28	7

Chain B: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	2-8	7
α-helix	10-17	8
α-helix	19-29	11

Chain C: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	2-5	4
α-helix	10-20	11
α-helix	22-29	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
human collagen type II	A, B, C	protein	31	Homo sapiens	P08123 (AlphaFold model)

Sequence of entity 1 (A, B, C), FASTA

>6JEC_1 human collagen type II (chains A, B, C)
XPPGPPGPPGRAGEPGLQGPAGPPGPPGPPG

Primary citation

Structure of a triple-helix region of human collagen type II. Yang, X., Zhu, Y., Ye, S. et al. To be published.

Other PDB entries of the same protein (UniProt P08123 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5CTD 1.6 Å, Crystal structure of the type IX collagen NC2 hetero-trimerization domain with a guest…
8YV3 1.68 Å, The heterotrimer structure of peptides derived from human collagen type I
5CTI 1.9 Å, Crystal structure of the type IX collagen NC2 hetero-trimerization domain with a guest…
5CVA 2.1 Å, Crystal structure of the type IX collagen NC2 hetero-trimerization domain with a guest…

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