Research workbench
Crystal structure of barley grain peroxidase 1
Analyse Crystal structure of barley grain peroxidase 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1BGP
- Type
- protein
- Length
- 309 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Barley grain peroxidase
- EC
- 1.11.1.7
- UniProt
- Q40069
- Ligands
- HEM, CA, NA
- Pockets
- 1 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Barley grain peroxidase (EC 1.11.1.7) | protein | 309 | 50% helix, 5% strand | Q40069 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- CA · Calcium ion · metal · chains A
- NA · Sodium ion · metal · 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 | 367 | 0.80 | 0.89 | 46 | HEM |
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 1BGP · Crystal structure of barley grain peroxidase 1 · 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 Q40069
- Elsewhere: RCSB PDB 1BGP · PDBe 1BGP · UniProt Q40069
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