Research workbench
Human formylglycine generating enzyme, C336S mutant, bromide co- crystallization
Analyse Human formylglycine generating enzyme, C336S mutant, bromide co- crystallization in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2HI8
- Type
- protein
- Length
- 279 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sulfatase-modifying factor 1; Ctpsr
- UniProt
- Q8NBK3
- Ligands
- NAG, CA, BR, CL
- Pockets
- 1 · best druggability 0.46
Structure
x-ray diffraction · 2 distinct chains · 16% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | Sulfatase-modifying factor 1 | protein | 274 | 16% helix, 21% strand | Q8NBK3 |
| P | Ctpsr | protein | 5 | 0% helix, 0% strand | — |
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
- BR · Bromide ion · ion · 15 copies · chains X, P
- CL · Chloride ion · ion · chains X, P
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 95 | 0.46 | 0.80 | 19 | empty |
Interfaces
1 interface between chains.
- X–P · 534 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide, 1 glycan (disulfide, N-glycosylation).
Compared structures
- 2HI8 · human formylglycine generating enzyme, C336S mutant, bromide co-crystallization · the same entry in another collection · chain X against X, TM-score 1.00
- Q8NBK3 · AlphaFold monomer V2.0 prediction for formylglycine-generating enzyme (Q8NBK3) · a predicted model of the same protein · chain X 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 Q8NBK3
- Elsewhere: RCSB PDB 2HI8 · PDBe 2HI8 · UniProt Q8NBK3
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