Research workbench
Asymmetric sulfoxidation by engineering the heme pocket of a dye- decolorizing peroxidase
Analyse Asymmetric sulfoxidation by engineering the heme pocket of a dye- decolorizing… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5IKG
- Type
- protein
- Length
- 445 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dye-decolorizing peroxidase
- EC
- 1.11.1.19
- UniProt
- I2DBY1
- Ligands
- HEM
- Pockets
- 1 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dye-decolorizing peroxidase (EC 1.11.1.19) | protein | 445 | 32% helix, 19% strand | I2DBY1 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
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 | 714 | 0.84 | 0.87 | 72 | HEM |
Compared structures
- 5IKG · Asymmetric sulfoxidation by engineering the heme pocket of a dye-decolorizing peroxidase · the same entry in another collection · chain A against A, TM-score 1.00
- I2DBY1 · AlphaFold monomer V2.0 prediction for dye-decolorizing peroxidase AAUDYP1 (I2DBY1) · a predicted model of the same protein · 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 I2DBY1
- Elsewhere: RCSB PDB 5IKG · PDBe 5IKG · UniProt I2DBY1
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