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Structure of horseradish peroxidase C1A compound III
Analyse Structure of horseradish peroxidase C1A compound III in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1H57
- Type
- protein
- Length
- 306 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peroxidase C1A
- EC
- 1.11.1.7
- UniProt
- P00433
- Ligands
- PEO, HEM, CA, OXY
- Pockets
- 1 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 49% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peroxidase C1A (EC 1.11.1.7) | protein | 306 | 49% helix, 5% strand | P00433 |
Ligands and binding sites
- PEO · Hydrogen peroxide · ligand · 3 copies · chains A
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- CA · Calcium ion · metal · 2 copies · chains A
- OXY · Oxygen molecule · ion · chains A
- ACT · Acetate ion · additive · 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 | 333 | 0.81 | 0.91 | 48 | HEM, OXY, PEO |
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
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 P00433
- Elsewhere: RCSB PDB 1H57 · PDBe 1H57 · UniProt P00433
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