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Crystal structure determination of CYS2ALA mutant of bile salt hydrolase from enterococcus feacalis

Analyse Crystal structure determination of CYS2ALA mutant of bile salt hydrolase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5GS7
Type
protein
Length
646 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Choloylglycine hydrolase
EC
3.5.1.24
UniProt
Q8KUA7
Pockets
9 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 19% helix, 33% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BCholoylglycine hydrolase (EC 3.5.1.24)protein32319% helix, 33% strandQ8KUA7

Pockets

9 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12820.770.8932empty
23150.750.8634empty
31010.440.7821empty
4780.440.8118empty
5620.420.8219empty

Interfaces

1 interface between chains.

  • A–B · 3187 Ų buried · 60 hydrogen bonds · protein-protein

Compared structures

  • 5GS7 · Crystal structure determination of Cys2Ala mutant of Bile Salt Hydrolase from… · the same entry in another collection · chain A against A, TM-score 1.00

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