1BKV: Collagen

Collagen. Determined by X-ray diffraction at 2.0 Å resolution. Released 16 Feb 1999.

Method: X-ray diffraction
Resolution: 2.0 Å
Chains: 3
Atoms: 692
Mol. weight: 8.36 kDa
Released: 16 Feb 1999

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

Secondary structure: helices and β-sheets

1BKV contains 5 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: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	7-20	14

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	37-56	20

Chain C: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	62-77	16
α-helix	79-83	5
α-helix	85-89	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
T3-785	A, B, C	protein	30

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

>1BKV_1 T3-785 (chains A, B, C)
PPGPPGPPGITGARGLAGPPGPPGPPGPPG

Primary citation

Sequence dependent conformational variations of collagen triple-helical structure. Kramer, R.Z., Bella, J., Mayville, P. et al. Nat Struct Biol (1999) 6:454-457. DOI 10.1038/8259 · PubMed

Browse more

1BKV is part of these collections:

Classic small proteins for teaching

About this viewer

MolViewer shows 1BKV directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.