The Crystal Structure of Human Leucine Carboxyl Methyltransferase 1. Determined by X-ray diffraction at 2.0 Å resolution. Released 8 Sept 2010.
Explore 3O7W in 3D Show helices and sheets RCSB PDB PDBe
3O7W contains 15 α-helices and 8 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 33-43 | 11 | |
| α-helix | 51-53 | 3 | |
| α-helix | 56-58 | 3 | |
| α-helix | 64-88 | 25 | |
| β-strand | 93-97 | 5 | 1 |
| α-helix | 104-110 | 7 | |
| β-strand | 117-122 | 6 | 1 |
| α-helix | 124-136 | 13 | |
| α-helix | 138-146 | 9 | |
| β-strand | 159-161 | 3 | 1 |
| β-strand | 165-169 | 5 | 1 |
| α-helix | 175-184 | 10 | |
| β-strand | 193-198 | 6 | 1 |
| α-helix | 201-203 | 3 | |
| α-helix | 206-219 | 14 | |
| β-strand | 223-230 | 8 | 1 |
| α-helix | 261-269 | 9 | |
| β-strand | 275-280 | 6 | 1 |
| α-helix | 281-286 | 6 | |
| α-helix | 290-297 | 8 | |
| α-helix | 308-312 | 5 | |
| β-strand | 315-322 | 8 | 1 |
| α-helix | 329-331 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Leucine carboxyl methyltransferase 1 | A | protein | 294 | Homo sapiens | Q9UIC8 (AlphaFold model) |
>3O7W_1 Leucine carboxyl methyltransferase 1 (chains A) GAMDENDEGVRGTCEDASLCKRFAVSIGYWHDPYIQHFVRLSKERKAPEINRGYFARVHG VSQLIKAFLRKTECHCQIVNLGAGMDTTFWRLKDEDLLPSKYFEVDFPMIVTRKLHSIKC KPPLSSPILELHSEDTLQMDGHILDSKRYAVIGADLRDLSELEEKLKKCNMNTQLPTLLI AECVLVYMTPEQSANLLKWAANSFERAMFINYEQVNEGKSLESQKERLLSNGWETASAVD MMELYNRLPRAEVSRIESLEFLDEMELLEQLMRHYCLCWATKGGNELGLKEITY
| ID | Name | Formula | Copies |
|---|---|---|---|
| SAM | S-adenosylmethionine | C15 H22 N6 O5 S | 1 |
Water and common crystallization additives (GOL, NA) are not listed.
The structure of human leucine carboxyl methyltransferase 1 that regulates protein phosphatase PP2A. Tsai, M.L., Cronin, N., Djordjevic, S. Acta Crystallogr D Biol Crystallogr (2011) 67:14-24. DOI 10.1107/S0907444910042204 · PubMed
Other PDB entries of the same protein (UniProt Q9UIC8 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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