Research workbench
Crystal structure of methylornithine synthase (pylb)
Analyse Crystal structure of methylornithine synthase (pylb) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3T7V
- Type
- protein
- Length
- 337 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Methylornithine synthase pylb
- EC
- 2.8.1.6
- UniProt
- Q46E78
- Ligands
- SF4, SAM, MD0
- Pockets
- 3 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Methylornithine synthase pylb (EC 2.8.1.6) | protein | 337 | 44% helix, 16% strand | Q46E78 |
Ligands and binding sites
- SF4 · Iron/sulfur cluster · ligand · chains A
- SAM · S-adenosylmethionine · ligand · chains A
- MD0 · 5-amino-D-isoleucine · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 323 | 0.86 | 0.95 | 43 | SF4, SAM, MD0 |
| 2 | 60 | 0.29 | 0.74 | 16 | empty |
| 3 | 57 | 0.27 | 0.74 | 18 | empty |
Compared structures
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 Q46E78
- Elsewhere: RCSB PDB 3T7V · PDBe 3T7V · UniProt Q46E78
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.