3IEI: Human leucine carboxylmethyltransferase-1
Crystal structure of human leucine carboxylmethyltransferase-1 in complex with S-adenosyl homocysteine. Determined by X-ray diffraction at 1.9 Å resolution. Released 11 Aug 2010.
- Method
- X-ray diffraction
- Resolution
- 1.9 Å
- Organism
- Homo sapiens
- Chains
- 8
- Atoms
- 22,201
- Mol. weight
- 312.63 kDa
- Ligands
- SAH
- Released
- 11 Aug 2010
Explore 3IEI in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
3IEI contains 133 α-helices and 72 β-strands across 8 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: 16 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 28-43 | 16 | |
| α-helix | 51-53 | 3 | |
| α-helix | 64-87 | 24 | |
| β-strand | 93-97 | 5 | 1 |
| α-helix | 104-110 | 7 | |
| β-strand | 117-122 | 6 | 1 |
| α-helix | 124-136 | 13 | |
| α-helix | 138-147 | 10 | |
| β-strand | 154 | 1 | 1 |
| 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 | 236-246 | 11 | |
| α-helix | 255-259 | 5 | |
| α-helix | 261-269 | 9 | |
| β-strand | 275-280 | 6 | 1 |
| α-helix | 281-286 | 6 | |
| α-helix | 290-299 | 10 | |
| α-helix | 305-312 | 8 | |
| β-strand | 315-322 | 8 | 1 |
| α-helix | 329-331 | 3 | |
Chain B: 16 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 29-43 | 15 | |
| α-helix | 51-53 | 3 | |
| α-helix | 64-88 | 25 | |
| β-strand | 93-97 | 5 | 2 |
| α-helix | 104-110 | 7 | |
| β-strand | 117-122 | 6 | 2 |
| α-helix | 124-136 | 13 | |
| α-helix | 138-146 | 9 | |
| β-strand | 154 | 1 | 2 |
| β-strand | 159-161 | 3 | 2 |
| β-strand | 165-169 | 5 | 2 |
| α-helix | 175-184 | 10 | |
| β-strand | 193-198 | 6 | 2 |
| α-helix | 201-203 | 3 | |
| α-helix | 206-219 | 14 | |
| β-strand | 223-230 | 8 | 2 |
| α-helix | 236-247 | 12 | |
| α-helix | 255-259 | 5 | |
| α-helix | 261-269 | 9 | |
| β-strand | 275-280 | 6 | 2 |
| α-helix | 281-286 | 6 | |
| α-helix | 290-299 | 10 | |
| α-helix | 306-312 | 7 | |
| β-strand | 315-322 | 8 | 2 |
| α-helix | 329-331 | 3 | |
Chain C: 17 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 28-42 | 15 | |
| α-helix | 51-53 | 3 | |
| α-helix | 56-58 | 3 | |
| α-helix | 64-88 | 25 | |
| β-strand | 93-97 | 5 | 3 |
| α-helix | 104-110 | 7 | |
| β-strand | 117-122 | 6 | 3 |
| α-helix | 124-136 | 13 | |
| α-helix | 138-147 | 10 | |
| β-strand | 154-156 | 3 | 3 |
| β-strand | 159-161 | 3 | 3 |
| β-strand | 165-169 | 5 | 3 |
| α-helix | 175-184 | 10 | |
| β-strand | 193-198 | 6 | 3 |
| α-helix | 201-203 | 3 | |
| α-helix | 206-219 | 14 | |
| β-strand | 223-230 | 8 | 3 |
| α-helix | 236-247 | 12 | |
| α-helix | 255-259 | 5 | |
| α-helix | 261-269 | 9 | |
| β-strand | 275-280 | 6 | 3 |
| α-helix | 281-286 | 6 | |
| α-helix | 290-297 | 8 | |
| α-helix | 306-312 | 7 | |
| β-strand | 315-322 | 8 | 3 |
| α-helix | 329-331 | 3 | |
Chain D: 17 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 26-28 | 3 | |
| α-helix | 29-43 | 15 | |
| α-helix | 51-53 | 3 | |
| α-helix | 64-87 | 24 | |
| β-strand | 93-97 | 5 | 4 |
| α-helix | 104-110 | 7 | |
| β-strand | 117-122 | 6 | 4 |
| α-helix | 124-136 | 13 | |
| α-helix | 138-146 | 9 | |
| β-strand | 154 | 1 | 4 |
| β-strand | 159-161 | 3 | 4 |
| β-strand | 165-169 | 5 | 4 |
| α-helix | 175-184 | 10 | |
| β-strand | 193-198 | 6 | 4 |
| α-helix | 201-203 | 3 | |
| α-helix | 206-219 | 14 | |
| β-strand | 223-230 | 8 | 4 |
| α-helix | 236-247 | 12 | |
| α-helix | 255-258 | 4 | |
| α-helix | 261-269 | 9 | |
| β-strand | 275-280 | 6 | 4 |
| α-helix | 281-286 | 6 | |
| α-helix | 290-298 | 9 | |
| α-helix | 306-312 | 7 | |
| β-strand | 315-322 | 8 | 4 |
| α-helix | 329-331 | 3 | |
Chain E: 17 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 26-28 | 3 | |
| α-helix | 29-43 | 15 | |
| α-helix | 51-53 | 3 | |
| α-helix | 64-88 | 25 | |
| β-strand | 93-97 | 5 | 5 |
| α-helix | 104-110 | 7 | |
| β-strand | 117-122 | 6 | 5 |
| α-helix | 124-136 | 13 | |
| α-helix | 138-147 | 10 | |
| β-strand | 155-156 | 2 | 5 |
| β-strand | 159-161 | 3 | 5 |
| β-strand | 165-169 | 5 | 5 |
| α-helix | 175-184 | 10 | |
| β-strand | 193-198 | 6 | 5 |
| α-helix | 201-203 | 3 | |
| α-helix | 206-219 | 14 | |
| β-strand | 223-230 | 8 | 5 |
| α-helix | 236-247 | 12 | |
| α-helix | 255-258 | 4 | |
| α-helix | 261-269 | 9 | |
| β-strand | 275-280 | 6 | 5 |
| α-helix | 281-286 | 6 | |
| α-helix | 290-297 | 8 | |
| α-helix | 306-312 | 7 | |
| β-strand | 315-322 | 8 | 5 |
| α-helix | 329-331 | 3 | |
Chain F: 16 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 28-43 | 16 | |
| α-helix | 51-53 | 3 | |
| α-helix | 64-87 | 24 | |
| β-strand | 93-97 | 5 | 6 |
| α-helix | 104-110 | 7 | |
| β-strand | 117-122 | 6 | 6 |
| α-helix | 124-136 | 13 | |
| α-helix | 138-147 | 10 | |
| β-strand | 154-156 | 3 | 6 |
| β-strand | 159-161 | 3 | 6 |
| β-strand | 165-169 | 5 | 6 |
| α-helix | 175-184 | 10 | |
| β-strand | 193-198 | 6 | 6 |
| α-helix | 201-203 | 3 | |
| α-helix | 206-219 | 14 | |
| β-strand | 223-230 | 8 | 6 |
| α-helix | 236-247 | 12 | |
| α-helix | 255-259 | 5 | |
| α-helix | 261-269 | 9 | |
| β-strand | 275-280 | 6 | 6 |
| α-helix | 281-286 | 6 | |
| α-helix | 290-297 | 8 | |
| α-helix | 306-312 | 7 | |
| β-strand | 315-322 | 8 | 6 |
| α-helix | 329-331 | 3 | |
Chain G: 17 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 28-43 | 16 | |
| α-helix | 51-53 | 3 | |
| α-helix | 56-58 | 3 | |
| α-helix | 64-88 | 25 | |
| β-strand | 93-97 | 5 | 7 |
| α-helix | 104-110 | 7 | |
| β-strand | 117-122 | 6 | 7 |
| α-helix | 124-136 | 13 | |
| α-helix | 138-145 | 8 | |
| β-strand | 154 | 1 | 7 |
| β-strand | 159-161 | 3 | 7 |
| β-strand | 165-169 | 5 | 7 |
| α-helix | 175-184 | 10 | |
| β-strand | 193-198 | 6 | 7 |
| α-helix | 201-203 | 3 | |
| α-helix | 206-219 | 14 | |
| β-strand | 223-230 | 8 | 7 |
| α-helix | 236-247 | 12 | |
| α-helix | 255-259 | 5 | |
| α-helix | 261-269 | 9 | |
| β-strand | 275-280 | 6 | 7 |
| α-helix | 281-286 | 6 | |
| α-helix | 290-299 | 10 | |
| α-helix | 305-312 | 8 | |
| β-strand | 315-322 | 8 | 7 |
| α-helix | 329-331 | 3 | |
Chain H: 17 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 26-28 | 3 | |
| α-helix | 29-43 | 15 | |
| α-helix | 51-53 | 3 | |
| α-helix | 64-88 | 25 | |
| β-strand | 93-97 | 5 | 8 |
| α-helix | 104-110 | 7 | |
| β-strand | 117-122 | 6 | 8 |
| α-helix | 124-136 | 13 | |
| α-helix | 138-147 | 10 | |
| β-strand | 154-156 | 3 | 8 |
| β-strand | 159-161 | 3 | 8 |
| β-strand | 165-169 | 5 | 8 |
| α-helix | 175-184 | 10 | |
| β-strand | 193-198 | 6 | 8 |
| α-helix | 201-203 | 3 | |
| α-helix | 206-219 | 14 | |
| β-strand | 223-230 | 8 | 8 |
| α-helix | 236-247 | 12 | |
| α-helix | 255-258 | 4 | |
| α-helix | 261-269 | 9 | |
| β-strand | 275-280 | 6 | 8 |
| α-helix | 281-286 | 6 | |
| α-helix | 290-297 | 8 | |
| α-helix | 305-312 | 8 | |
| β-strand | 315-322 | 8 | 8 |
| α-helix | 329-331 | 3 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Leucine carboxyl methyltransferase 1 | A, B, C, D, E, F, G, H | protein | 334 | Homo sapiens | Q9UIC8 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E, F, G, H), FASTA
>3IEI_1 Leucine carboxyl methyltransferase 1 (chains A, B, C, D, E, F, G, H)
MATRQRESSITSCCSTSSMDENDEGVRGTCEDASLCKRFAVSIGYWHDPYIQHFVRLSKE
RKAPEINRGYFARVHGVSQLIKAFLRKTECHCQIVNLGAGMDTTFWRLKDEDLLSSKYFE
VDFPMIVTRKLHSIKCKPPLSSPILELHSEDTLQMDGHILDSKRYAVIGADLRDLSELEE
KLKKCNMNTQLPTLLIAECVLVYMTPEQSANLLKWAANSFERAMFINYEQVNMGDRFGQI
MIENLRRRQCDLAGVETCKSLESQKERLLSNGWETASAVDMMELYNRLPRAEVSRIESLE
FLDEMELLEQLMRHYCLCWATKGGNELGLKEITY
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| SAH | S-adenosyl-L-homocysteine | C14 H20 N6 O5 S | 8 |
Water and common crystallization additives (MES, GOL) are not listed.
Primary citation
Structural Insights into Novel Functions of a pro-survival PP2A-specific Methyltransferase. Stanevich, V., Jiang, L., Satyshur, K.A. et al. To be published.
Other PDB entries of the same protein (UniProt Q9UIC8 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 3O7W 2.0 Å, The Crystal Structure of Human Leucine Carboxyl Methyltransferase 1
- 3P71 2.7 Å, Crystal structure of the complex of LCMT-1 and PP2A
Browse structure collections
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