MolNFT v2 · #122610 · protein
Asymmetric sulfoxidation by engineering the heme pocket of a dye-decolorizing peroxidase
5IKG: “Asymmetric sulfoxidation by engineering the heme pocket of a dye-decolorizing peroxidase”. X-ray diffraction at 1.95, 1 ligand (HEM). MolNFT v2 #122610 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5IKG
- Type
- protein
- Length
- 445 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.95
- Source
- Auricularia auricula-judae
- UniProt
- I2DBY1
- Ligands
- HEM
Structure
x-ray diffraction · resolution 1.95 · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 445 | — | 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.
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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