Research workbench
The crystal structure of engineered cytochrome C peroxidase from saccharomyces cerevisiae with TRP51 to S-TRP51 and TRP191PHE modifications
Analyse The crystal structure of engineered cytochrome C peroxidase from saccharomyces… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6Y2Y
- Type
- protein
- Length
- 295 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome C peroxidase, mitochondrial
- EC
- 1.11.1.5
- UniProt
- P00431
- Ligands
- HEM
- Pockets
- 2 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome C peroxidase, mitochondrial (EC 1.11.1.5) | protein | 295 | 48% helix, 9% strand | P00431 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- EDO · 1,2-ethanediol · additive · 4 copies · chains A
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 | 380 | 0.79 | 0.88 | 44 | HEM |
| 2 | 84 | 0.38 | 0.77 | 19 | EDO |
Modifications
Observed in the structure: 1 modified (nonstandard).
Compared structures
- 6Y2Y · The crystal structure of engineered cytochrome c peroxidase from Saccharomyces cerevisiae… · the same entry in another collection · chain A against A, TM-score 1.00
- P00431 · AlphaFold monomer V2.0 prediction for cytochrome C peroxidase, mitochondrial (P00431) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P00431
- Elsewhere: RCSB PDB 6Y2Y · PDBe 6Y2Y · UniProt P00431
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