Research workbench
The crystal structure of human leucine carboxyl methyltransferase 1
Analyse The crystal structure of human leucine carboxyl methyltransferase 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3O7W
- Type
- protein
- Length
- 282 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Leucine carboxyl methyltransferase 1
- EC
- 2.1.1.-
- UniProt
- Q9UIC8
- Ligands
- SAM, NA
- Pockets
- 2 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Leucine carboxyl methyltransferase 1 (EC 2.1.1.-) | protein | 282 | 45% helix, 17% strand | Q9UIC8 |
Ligands and binding sites
- SAM · S-adenosylmethionine · ligand · chains A
- NA · Sodium ion · metal · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 368 | 0.66 | 0.80 | 48 | SAM |
| 2 | 125 | 0.51 | 0.81 | 27 | empty |
Compared structures
- 3O7W · The Crystal Structure of Human Leucine Carboxyl Methyltransferase 1 · the same entry in another collection · chain A against A, TM-score 1.00
- Q9UIC8 · AlphaFold monomer V2.0 prediction for leucine carboxyl methyltransferase 1 (Q9UIC8) · a predicted model of the same protein · chain A against A, TM-score 0.98
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q9UIC8
- Elsewhere: RCSB PDB 3O7W · PDBe 3O7W · UniProt Q9UIC8
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