Research workbench
Arabidopsis thaliana peroxidase A2 at room temperature
Analyse Arabidopsis thaliana peroxidase A2 at room temperature in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QO4
- Type
- protein
- Length
- 306 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peroxidase
- EC
- 1.11.1.7
- UniProt
- Q42578
- Ligands
- HEM, CA
- Pockets
- 2 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peroxidase (EC 1.11.1.7) | protein | 306 | 50% helix, 4% strand | Q42578 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- CA · Calcium ion · metal · 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 | 361 | 0.80 | 0.90 | 52 | HEM |
| 2 | 55 | 0.28 | 0.74 | 15 | 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 Q42578
- Elsewhere: RCSB PDB 1QO4 · PDBe 1QO4 · UniProt Q42578
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