Research workbench
Formylglycine generating enzyme C341S mutant
Analyse Formylglycine generating enzyme C341S mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2AFY
- Type
- protein
- Length
- 274 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sulfatase modifying factor 1
- UniProt
- Q8NBK3
- Ligands
- NAG, CA
- Pockets
- 2 · best druggability 0.53
Structure
x-ray diffraction · 1 distinct chain · 16% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | Sulfatase modifying factor 1 | protein | 274 | 16% helix, 20% strand | Q8NBK3 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains X
- CA · Calcium ion · metal · 2 copies · chains X
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 176 | 0.53 | 0.79 | 22 | empty |
| 2 | 112 | 0.49 | 0.80 | 20 | empty |
Modifications
Observed in the structure: 2 disulfide, 1 glycan, 1 modified (disulfide, N-glycosylation, oxidation).
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 Q8NBK3
- Elsewhere: RCSB PDB 2AFY · PDBe 2AFY · UniProt Q8NBK3
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