Research workbench
Lignin peroxidase H8 triple mutant S49C/A67C/H239
Analyse Lignin peroxidase H8 triple mutant S49C/A67C/H239 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ISS
- Type
- protein
- Length
- 692 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ligninase H8
- EC
- 1.11.1.14
- UniProt
- P06181
- Ligands
- HEM, CA
- Pockets
- 3 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ligninase H8 (EC 1.11.1.14) | protein | 345 | 41% helix, 7% strand | P06181 |
| G | Ligninase H8 (EC 1.11.1.14) | protein | 347 | 40% helix, 7% strand | P06181 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, G
- CA · Calcium ion · metal · 4 copies · chains A, G
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 377 | 0.84 | 0.92 | 49 | HEM |
| 2 | 377 | 0.83 | 0.91 | 46 | HEM |
| 3 | 852 | 0.80 | 0.83 | 71 | empty |
Interfaces
1 interface between chains.
- A–G · 625 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 disulfide, 2 modified (disulfide, hydroxylation).
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 6ISS · PDBe 6ISS · UniProt P06181
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