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Crystal structure of the C90A mutant of the sco copper chaperone protein from streptomyces lividans

Analyse Crystal structure of the C90A mutant of the sco copper chaperone protein from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4BPY
Type
protein
Length
163 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Sco protein
UniProt
Q93J40
Pockets
1 · best druggability 0.28

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASco proteinprotein16334% helix, 24% strandQ93J40

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1530.280.7415empty

Modifications

Observed in the structure: 1 modified (oxidation).

Compared structures

  • 4BPY · Crystal structure of the C90A mutant of the Sco copper chaperone protein from… · the same entry in another collection · chain A against A, TM-score 1.00

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