Research workbench
Di-haem cytochrome C peroxidase, form out
Analyse Di-haem cytochrome C peroxidase, form out in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1RZ5
- Type
- protein
- Length
- 309 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome C peroxidase
- EC
- 1.11.1.5
- UniProt
- P83787
- Ligands
- HEC, CA
- Pockets
- 2 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome C peroxidase (EC 1.11.1.5) | protein | 309 | 39% helix, 8% strand | P83787 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 280 | 0.82 | 0.93 | 41 | HEC |
| 2 | 507 | 0.78 | 0.85 | 61 | HEC |
Modifications
Observed in the structure: 4 cofactor (heme c attachment).
Compared structures
- 1RZ5 · Di-haem Cytochrome c Peroxidase, Form OUT · 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 P83787
- Elsewhere: RCSB PDB 1RZ5 · PDBe 1RZ5 · UniProt P83787
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