Research workbench
Laccase from streptomyces coelicolor
Analyse Laccase from streptomyces coelicolor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3CG8
- Type
- protein
- Length
- 814 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Laccase
- EC
- 1.10.3.2
- UniProt
- Q9XAL8
- Ligands
- CU, O
- Pockets
- 8 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 6% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Laccase (EC 1.10.3.2) | protein | 270 | 6% helix, 42% strand | Q9XAL8 |
| B, C | Laccase (EC 1.10.3.2) | protein | 272 | 5% helix, 43% strand | Q9XAL8 |
Ligands and binding sites
- CU · Copper (II) ion · metal · 12 copies · chains A, C, B
- O · Oxygen atom · ion · 3 copies · chains A, C, B
- PG4 · Tetraethylene glycol · additive · 5 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 424 | 0.84 | 0.92 | 74 | empty |
| 2 | 165 | 0.52 | 0.79 | 29 | empty |
| 3 | 142 | 0.51 | 0.80 | 29 | empty |
| 4 | 170 | 0.51 | 0.78 | 27 | empty |
| 5 | 71 | 0.36 | 0.77 | 16 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1843 Ų buried · 35 hydrogen bonds · protein-protein
- B–C · 1836 Ų buried · 31 hydrogen bonds · protein-protein
- A–C · 1810 Ų buried · 35 hydrogen bonds · protein-protein
Compared structures
- 3CG8 · Laccase from Streptomyces coelicolor · 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 Q9XAL8
- Elsewhere: RCSB PDB 3CG8 · PDBe 3CG8 · UniProt Q9XAL8
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