Three-Dimensional Solution Structure of Apo-Mts1. Determined by solution NMR. Released 30 Oct 2002.
Explore 1M31 in 3D Show helices and sheets RCSB PDB PDBe
1M31 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-23 | 20 | |
| β-strand | 29-30 | 2 | 1 |
| α-helix | 31-41 | 11 | |
| α-helix | 44-47 | 4 | |
| α-helix | 52-62 | 11 | |
| β-strand | 69-70 | 2 | 1 |
| α-helix | 72-85 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Placental calcium-binding protein | A, B | protein | 101 | Homo sapiens | P26447 (AlphaFold model) |
>1M31_1 Placental calcium-binding protein (chains A, B) MACPLEKALDVMVSTFHKYSGKEGDKFKLNKSELKELLTRELPSFLGKRTDEAAFQKLMS NLDSNRDNEVDFQEYCVFLSCIAMMCNEFFEGFPDKQPRKK
Solution structure of human Mts1 (S100A4) as determined by NMR spectroscopy. Vallely, K.M., Rustandi, R.R., Ellis, K.C. et al. Biochemistry (2002) 41:12670-12680. DOI 10.1021/bi020365r · PubMed
Other PDB entries of the same protein (UniProt P26447 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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