3CGA: Protein S100-A4

Crystal structure of metastasis-associated protein S100A4 in the active, calcium-bound form. Determined by X-ray diffraction at 2.03 Å resolution. Released 30 Sept 2008.

Method
X-ray diffraction
Resolution
2.03 Å
Organism
Homo sapiens
Chains
2
Atoms
1,467
Mol. weight
23.65 kDa
Ligands
CA
Released
30 Sept 2008

Explore 3CGA in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3CGA contains 10 α-helices and 4 β-strands across 2 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: 5 helices, 2 β-strands

ElementResiduesLengthSheet
α-helix5-2016
β-strand28-2921
α-helix31-4111
α-helix43-453
α-helix54-629
β-strand70-7121
α-helix72-8817
Chain B: 5 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix5-2016
β-strand28-2922
α-helix31-4111
α-helix44-463
α-helix53-608
β-strand70-7122
α-helix72-8918

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Protein S100-A4A, Bprotein101Homo sapiensP26447 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>3CGA_1 Protein S100-A4 (chains A, B)
MACPLEKALDVMVSTFHKYSGKEGDKFKLNKSELKELLTRELPSFLGKRTDEAAFQKLMS
NLDSNRDNEVDFQEYCVFLSCIAMMCNEFFEGFPDKQPRKK

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa4

Primary citation

Crystal structure of metastasis-associated protein S100A4 in the active calcium-bound form. Pathuri, P., Vogeley, L., Luecke, H. J Mol Biol (2008) 383:62-77. DOI 10.1016/j.jmb.2008.04.076 · PubMed

Other PDB entries of the same protein (UniProt P26447 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

MolViewer shows 3CGA 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.