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The crystal structure of the S154Y mutant carbonyl reductase from leifsonia xyli explains enhanced activity for 3,5- BIS(TRIFLUOROMETHYL)ACETOPHENONE reduction

Analyse The crystal structure of the S154Y mutant carbonyl reductase from leifsonia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6XNB
Type: protein
Length: 251 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Short chain alcohol dehydrogenase
UniProt: T2FLN4
Ligands: MG
Pockets: 1 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Short chain alcohol dehydrogenase	protein	251	51% helix, 17% strand	T2FLN4

Ligands and binding sites

MG · Magnesium ion · metal · 3 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	591	0.71	0.79	46	empty

Compared structures

6XNB · The Crystal Structure of the S154Y Mutant Carbonyl Reductase from Leifsonia xyli Explains… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt T2FLN4
Elsewhere: RCSB PDB 6XNB · PDBe 6XNB · UniProt T2FLN4

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