Research workbench
Crystal structure of multicopper oxidase
Analyse Crystal structure of multicopper oxidase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3GDC
- Type
- protein
- Length
- 859 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Multicopper oxidase
- EC
- 1.10.3.2
- UniProt
- A0AW19
- Ligands
- CU, CA
- Pockets
- 3 · best druggability 0.81
Structure
x-ray diffraction · 3 distinct chains · 9% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Multicopper oxidase (EC 1.10.3.2) | protein | 288 | 9% helix, 46% strand | A0AW19 |
| B | Multicopper oxidase (EC 1.10.3.2) | protein | 285 | 10% helix, 46% strand | A0AW19 |
| C | Multicopper oxidase (EC 1.10.3.2) | protein | 286 | 9% helix, 47% strand | A0AW19 |
Ligands and binding sites
- CU · Copper (II) ion · metal · 12 copies · chains A, C, B
- CA · Calcium ion · metal · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 400 | 0.81 | 0.90 | 59 | empty |
| 2 | 183 | 0.46 | 0.75 | 26 | empty |
| 3 | 63 | 0.36 | 0.78 | 14 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1248 Ų buried · 17 hydrogen bonds · protein-protein
- A–C · 1219 Ų buried · 18 hydrogen bonds · protein-protein
- B–C · 1218 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 3GDC · Crystal structure of multicopper oxidase · 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 A0AW19
- Elsewhere: RCSB PDB 3GDC · PDBe 3GDC · UniProt A0AW19
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