2LLP: THP type 1 alpha 1 collagen fragment

Solution structure of a THP type 1 alpha 1 collagen fragment (772-786). Determined by solution NMR. Released 30 May 2012.

Method
Solution NMR
Organism
Homo sapiens
Chains
3
Atoms
313
Mol. weight
4.97 kDa
Released
30 May 2012

Explore 2LLP in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2LLP contains 5 α-helices and 3 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, 1 β-strand

ElementResiduesLengthSheet
β-strand1611
α-helix17-2610
Chain B: 2 helices, 1 β-strand
ElementResiduesLengthSheet
α-helix151
β-strand1611
α-helix17-248
Chain C: 2 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand1611
α-helix17-193
α-helix21-233

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Collagen alpha-1(I) chainA, B, Cprotein18Homo sapiensP02452 (AlphaFold model)
Sequence of entity 1 (A, B, C), FASTA
>2LLP_1 Collagen alpha-1(I) chain (chains A, B, C)
PPGPQGIAGQRGVVGLPG

Primary citation

Structural basis for matrix metalloproteinase 1-catalyzed collagenolysis. Bertini, I., Fragai, M., Luchinat, C. et al. J Am Chem Soc (2012) 134:2100-2110. DOI 10.1021/ja208338j · PubMed

Other PDB entries of the same protein (UniProt P02452 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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