MolNFT v1 · #109143 · protein
Structure of the SSL1 laccase mutant M295L
4WTQ · Copper oxidase: “Structure of the SSL1 laccase mutant M295L”. X-ray diffraction, 2 ligands (CU, O), 7 pockets (best druggability 0.83). MolNFT v1 #109143 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4WTQ
- Type
- protein
- Length
- 808 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Copper oxidase
- EC
- 1.10.3.2
- UniProt
- B5HSR1
- Ligands
- CU, O
- Pockets
- 7 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 5% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Copper oxidase (EC 1.10.3.2) | protein | 270 | 5% helix, 42% strand | B5HSR1 |
| B, C | Copper oxidase (EC 1.10.3.2) | protein | 269 | 5% helix, 43% strand | B5HSR1 |
Ligands and binding sites
- CU · Copper (II) ion · metal · 9 copies · chains A, B, C
- O · Oxygen atom · ion · 2 copies · chains A, B, C
- GOL · Glycerol · additive · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 358 | 0.83 | 0.92 | 61 | empty |
| 2 | 229 | 0.69 | 0.86 | 52 | empty |
| 3 | 222 | 0.67 | 0.85 | 52 | empty |
| 4 | 220 | 0.67 | 0.85 | 45 | empty |
| 5 | 107 | 0.37 | 0.74 | 15 | empty |
Interfaces
3 interfaces between chains.
- A–C · 1880 Ų buried · 35 hydrogen bonds · protein-protein
- A–B · 1810 Ų buried · 34 hydrogen bonds · protein-protein
- B–C · 1767 Ų buried · 31 hydrogen bonds · protein-protein
Compared structures
- 4WTQ · Structure of the Ssl1 laccase mutant M295L · 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 B5HSR1
- Elsewhere: RCSB PDB 4WTQ · PDBe 4WTQ · UniProt B5HSR1
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