Research workbench
Structure of ferric horseradish peroxidase C1A in complex with acetate
Analyse Structure of ferric horseradish peroxidase C1A in complex with acetate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1H5A
- 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
- HEM, CA
- Pockets
- 2 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peroxidase C1A (EC 1.11.1.7) | protein | 306 | 50% helix, 4% strand | P00433 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- CA · Calcium ion · metal · 2 copies · chains A
- ACT · Acetate ion · additive · 2 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 | 359 | 0.81 | 0.90 | 45 | HEM, ACT |
| 2 | 50 | 0.44 | 0.84 | 17 | empty |
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 1H5A · PDBe 1H5A · UniProt P00433
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