Research workbench
Crystal structure of sfmd truncated variant
Analyse Crystal structure of sfmd truncated variant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6VDP
- Type
- protein
- Length
- 304 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 3-methyl-L-tyrosine peroxygenase
- EC
- 1.11.2.5
- UniProt
- B0CN28
- Ligands
- HEC
- Pockets
- 6 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 61% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 3-methyl-L-tyrosine peroxygenase (EC 1.11.2.5) | protein | 304 | 61% helix, 3% strand | B0CN28 |
Ligands and binding sites
- HEC · Heme C · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 195 | 0.68 | 0.86 | 29 | HEC |
| 2 | 144 | 0.48 | 0.78 | 26 | empty |
| 3 | 58 | 0.44 | 0.83 | 18 | empty |
| 4 | 62 | 0.43 | 0.82 | 16 | empty |
| 5 | 73 | 0.38 | 0.78 | 20 | empty |
Modifications
Observed in the structure: 1 cofactor (heme c attachment).
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 B0CN28
- Elsewhere: RCSB PDB 6VDP · PDBe 6VDP · UniProt B0CN28
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.