Research workbench
Multicopper oxidase mglac (DATA4)
Analyse Multicopper oxidase mglac (DATA4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4E9Y
- Type
- protein
- Length
- 949 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Multicopper oxidase
- UniProt
- C0STU6
- Ligands
- CU, OXY, CL
- Pockets
- 10 · best druggability 0.86
Structure
x-ray diffraction · 2 distinct chains · 8% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Multicopper oxidase | protein | 317 | 8% helix, 45% strand | C0STU6 |
| B, C | Multicopper oxidase | protein | 316 | 7% helix, 45% strand | C0STU6 |
Ligands and binding sites
- CU · Copper (II) ion · metal · 12 copies · chains A, B, C
- OXY · Oxygen molecule · ion · 3 copies · chains A, C, B
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 400 | 0.86 | 0.94 | 42 | empty |
| 2 | 1100 | 0.82 | 0.83 | 63 | empty |
| 3 | 126 | 0.57 | 0.83 | 25 | empty |
| 4 | 97 | 0.51 | 0.82 | 19 | empty |
| 5 | 99 | 0.51 | 0.82 | 20 | empty |
Interfaces
3 interfaces between chains.
- B–C · 1656 Ų buried · 28 hydrogen bonds · protein-protein
- A–B · 1652 Ų buried · 32 hydrogen bonds · protein-protein
- A–C · 1596 Ų buried · 25 hydrogen bonds · protein-protein
Compared structures
- 4E9Y · Multicopper Oxidase mgLAC (data4) · 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 C0STU6
- Elsewhere: RCSB PDB 4E9Y · PDBe 4E9Y · UniProt C0STU6
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