MolNFT v1 · #125880 · protein
Crystal structure of a laccase-like multicopper oxidase mcog from from aspergillus niger
5LM8 · 'multicopper oxidase: “Crystal structure of a laccase-like multicopper oxidase mcog from from aspergillus niger”. X-ray diffraction, 5 ligands (NAG, BMA, MAN), 2 pockets (best druggability 0.55). MolNFT v1 #125880 on GenesisL1: 3D…
- PDB
- 5LM8
- Type
- protein
- Length
- 549 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 'multicopper oxidase
- EC
- 1.10.3.2
- UniProt
- A2QS62
- Ligands
- NAG, BMA, MAN, CU, PER
- Pockets
- 2 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 11% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 'multicopper oxidase (EC 1.10.3.2) | protein | 549 | 11% helix, 40% strand | A2QS62 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 9 copies · chains A
- BMA · beta-D-mannopyranose · sugar · 2 copies · chains A
- MAN · alpha-D-mannopyranose · sugar · 2 copies · chains A
- CU · Copper (II) ion · metal · 4 copies · chains A
- PER · Peroxide ion · ion · 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 118 | 0.55 | 0.82 | 29 | empty |
| 2 | 201 | 0.54 | 0.78 | 31 | NAG |
Modifications
Observed in the structure: 5 glycan, 2 disulfide (N-glycosylation, disulfide, glycosylation).
Compared structures
- 5LM8 · Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger · 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 A2QS62
- Elsewhere: RCSB PDB 5LM8 · PDBe 5LM8 · UniProt A2QS62
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