Research workbench
Pristine recomb. lignin peroxidase H8
Analyse Pristine recomb. lignin peroxidase H8 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1B82
- Type
- protein
- Length
- 694 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (lignin peroxidase)
- EC
- 1.11.1.14
- UniProt
- P06181
- Ligands
- HEM, CA
- Pockets
- 5 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (lignin peroxidase) (EC 1.11.1.14) | protein | 349 | 41% helix, 6% strand | P06181 |
| B | Protein (lignin peroxidase) (EC 1.11.1.14) | protein | 345 | 41% helix, 7% strand | P06181 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
- CA · Calcium ion · metal · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 389 | 0.84 | 0.92 | 48 | HEM |
| 2 | 384 | 0.83 | 0.91 | 49 | HEM |
| 3 | 214 | 0.43 | 0.72 | 27 | empty |
| 4 | 81 | 0.35 | 0.75 | 20 | empty |
| 5 | 75 | 0.34 | 0.75 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 88 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 8 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 P06181
- Elsewhere: RCSB PDB 1B82 · PDBe 1B82 · UniProt P06181
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