Research workbench
Structure of fructosyl peptide oxidase from E. terrenum
Analyse Structure of fructosyl peptide oxidase from E. terrenum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4RSL
- Type
- protein
- Length
- 436 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fructosyl peptide oxidase
- EC
- 1.5.3.-
- UniProt
- Q765A9
- Ligands
- FAD, PO4
- Pockets
- 1 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fructosyl peptide oxidase (EC 1.5.3.-) | protein | 436 | 31% helix, 26% strand | Q765A9 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1063 | 0.82 | 0.83 | 114 | FAD |
Compared structures
- 4RSL · Structure of fructosyl peptide oxidase from E. terrenum · 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 Q765A9
- Elsewhere: RCSB PDB 4RSL · PDBe 4RSL · UniProt Q765A9
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