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Crystal structure of two-domain laccase mutant H165A/M199G from streptomyces griseoflavus

Analyse Crystal structure of two-domain laccase mutant H165A/M199G from streptomyces… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7PU0
Type
protein
Length
1,664 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Two-domain laccase
EC
1.10.3.2
UniProt
A0A0M4FJ81
Ligands
CU, NA
Pockets
20 · best druggability 0.85

Structure

x-ray diffraction · 3 distinct chains · 6% helix, 42% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATwo-domain laccase (EC 1.10.3.2)protein2806% helix, 42% strandA0A0M4FJ81
B, D, ETwo-domain laccase (EC 1.10.3.2)protein2785% helix, 41% strandA0A0M4FJ81
C, FTwo-domain laccase (EC 1.10.3.2)protein2755% helix, 42% strandA0A0M4FJ81

Ligands and binding sites

  • CU · Copper (II) ion · metal · 24 copies · chains A, C, B, D, F, E
  • NA · Sodium ion · metal · 2 copies · chains B, C, D, F

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

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14050.850.9361NA
23810.840.9356NA
32960.770.8957empty
42280.760.9041empty
52060.740.9038empty

Interfaces

12 interfaces between chains.

  • A–C · 1832 Ų buried · 34 hydrogen bonds · protein-protein
  • A–B · 1803 Ų buried · 37 hydrogen bonds · protein-protein
  • D–F · 1776 Ų buried · 33 hydrogen bonds · protein-protein
  • D–E · 1764 Ų buried · 34 hydrogen bonds · protein-protein
  • B–C · 1757 Ų buried · 34 hydrogen bonds · protein-protein

Compared structures

  • 7PU0 · Crystal Structure of Two-Domain Laccase mutant H165A/M199G from Streptomyces griseoflavus · the same entry in another collection · chain A against A, TM-score 1.00

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