MolNFT v1 · #173600 · protein
Structure of the M298L mutant of the streptomyces coelicolor small laccase T1 copper axial ligand
7B4Y · Putative copper oxidase: “Structure of the M298L mutant of the streptomyces coelicolor small laccase T1 copper axial ligand”. X-ray diffraction, 1 ligand (CU), 5 pockets (best druggability 0.61). MolNFT v1 #173600 on GenesisL1: 3D…
- PDB
- 7B4Y
- Type
- protein
- Length
- 554 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative copper oxidase
- UniProt
- Q9XAL8
- Ligands
- CU
- Pockets
- 5 · best druggability 0.61
Structure
x-ray diffraction · 1 distinct chain · 5% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Putative copper oxidase | protein | 277 | 5% helix, 42% strand | Q9XAL8 |
Ligands and binding sites
- CU · Copper (II) ion · metal · 8 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 625 | 0.61 | 0.73 | 76 | empty |
| 2 | 54 | 0.31 | 0.76 | 14 | empty |
| 3 | 70 | 0.31 | 0.74 | 14 | empty |
| 4 | 67 | 0.29 | 0.74 | 15 | empty |
| 5 | 50 | 0.27 | 0.74 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1102 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 7B4Y · Structure of the M298L mutant of the Streptomyces coelicolor small laccase T1 copper… · 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 7B4Y · PDBe 7B4Y · UniProt Q9XAL8
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