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Structure of the M198F M298F double mutant of the streptomyces coelicolor small laccase T1 copper site

Analyse Structure of the M198F M298F double mutant of the streptomyces coelicolor small… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7BFM
Type
protein
Length
564 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Putative copper oxidase
UniProt
Q9XAL8
Ligands
CU
Pockets
4 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 6% helix, 41% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CPutative copper oxidaseprotein2826% helix, 41% strandQ9XAL8

Ligands and binding sites

  • CU · Copper (II) ion · metal · 8 copies · chains A, C
  • PG4 · Tetraethylene glycol · additive · 2 copies · chains A, C

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17580.630.7389empty
2700.310.7514empty
3640.310.7514empty
4520.270.7415empty

Interfaces

1 interface between chains.

  • A–C · 1155 Ų buried · 8 hydrogen bonds · protein-protein

Compared structures

  • 7BFM · Structure of the M198F M298F double mutant of the Streptomyces coelicolor small laccase… · the same entry in another collection · chain A against A, TM-score 1.00

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