Research workbench
Structure of polyphenol oxidase (mutant G292N) from thermothelomyces thermophila
Analyse Structure of polyphenol oxidase (mutant G292N) from thermothelomyces thermophila in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6Z1S
- Type
- protein
- Length
- 381 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrosinase-like protein
- UniProt
- G2QLD3
- Ligands
- GLY, SER, NAG, CU
- Pockets
- 5 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosinase-like protein | protein | 381 | 40% helix, 9% strand | G2QLD3 |
Ligands and binding sites
- GLY · Glycine · ligand · 6 copies · chains A
- SER · Serine · ligand · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A
- CU · Copper (II) ion · metal · 2 copies · chains A
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 437 | 0.67 | 0.79 | 48 | SER |
| 2 | 63 | 0.46 | 0.84 | 19 | GLY |
| 3 | 51 | 0.36 | 0.80 | 19 | empty |
| 4 | 80 | 0.36 | 0.76 | 14 | GLY |
| 5 | 54 | 0.32 | 0.77 | 13 | empty |
Modifications
Observed in the structure: 3 glycan, 2 disulfide (N-glycosylation, disulfide).
Compared structures
- 6Z1S · Structure of Polyphenol Oxidase (mutant G292N) from Thermothelomyces thermophila · 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 G2QLD3
- Elsewhere: RCSB PDB 6Z1S · PDBe 6Z1S · UniProt G2QLD3
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