1KS0: Matrix Metalloproteinase 2

The First Fibronectin Type II Module from Human Matrix Metalloproteinase 2. Determined by solution NMR. Released 20 Feb 2002.

Method
Solution NMR
Organism
Homo sapiens
Chains
1
Atoms
477
Mol. weight
7.28 kDa
Released
20 Feb 2002

Explore 1KS0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1KS0 contains 1 α-helix and 7 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: 1 helix, 7 β-strands

ElementResiduesLengthSheet
β-strand711
β-strand18-2032
β-strand23-2532
β-strand2911
β-strand39-4131
β-strand4512
α-helix46-494
β-strand52-5431

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Matrix Metalloproteinase 2Aprotein63Homo sapiensP08253 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1KS0_1 Matrix Metalloproteinase 2 (chains A)
RIPVKYGNADGEYCKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFCPHEAL
FTM

Primary citation

The col-1 module of human matrix metalloproteinase-2 (MMP-2): structural/functional relatedness between gelatin-binding fibronectin type II modules and lysine-binding kringle domains. Gehrmann, M., Briknarova, K., Banyai, L. et al. Biol Chem (2002) 383:137-148. DOI 10.1515/BC.2002.014 · PubMed

Other PDB entries of the same protein (UniProt P08253 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

MolViewer shows 1KS0 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.