Research workbench
Crystal structure of semet-substituted curj carbon methyltransferase
Analyse Crystal structure of semet-substituted curj carbon methyltransferase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5THY
- Type
- protein
- Length
- 763 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Curj
- UniProt
- F4Y426
- Ligands
- SAH, GDS
- Pockets
- 5 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 48% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Curj | protein | 387 | 48% helix, 16% strand | F4Y426 |
| B | Curj | protein | 376 | 49% helix, 17% strand | F4Y426 |
Ligands and binding sites
- SAH · S-adenosyl-L-homocysteine · ligand · 2 copies · chains A, B
- GDS · Oxidized glutathione disulfide · ligand · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 539 | 0.83 | 0.89 | 62 | SAH |
| 2 | 290 | 0.76 | 0.88 | 34 | SAH |
| 3 | 250 | 0.75 | 0.89 | 33 | empty |
| 4 | 88 | 0.50 | 0.83 | 28 | empty |
| 5 | 120 | 0.36 | 0.73 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 715 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 modified (engineered).
Compared structures
- 5THY · Crystal structure of SeMet-Substituted CurJ carbon methyltransferase · the same entry in another collection · chain A against A, TM-score 1.00
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 F4Y426
- Elsewhere: RCSB PDB 5THY · PDBe 5THY · UniProt F4Y426
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