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Sodium in PDB 7v8o: Crystal Structure of Cyclohexanone Monooxygenase From T. Municipale Mutant L437T Complexed with Nadp+ and Fad in Space Group of P21221

Enzymatic activity of Crystal Structure of Cyclohexanone Monooxygenase From T. Municipale Mutant L437T Complexed with Nadp+ and Fad in Space Group of P21221

All present enzymatic activity of Crystal Structure of Cyclohexanone Monooxygenase From T. Municipale Mutant L437T Complexed with Nadp+ and Fad in Space Group of P21221:
1.14.13.22;

Protein crystallography data

The structure of Crystal Structure of Cyclohexanone Monooxygenase From T. Municipale Mutant L437T Complexed with Nadp+ and Fad in Space Group of P21221, PDB code: 7v8o was solved by T.Li, G.Y.Li, H.Yin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.15 / 2.72
Space group P 21 2 21
Cell size a, b, c (Å), α, β, γ (°) 68.301, 112.522, 156.405, 90, 90, 90
R / Rfree (%) 22 / 28.1

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of Cyclohexanone Monooxygenase From T. Municipale Mutant L437T Complexed with Nadp+ and Fad in Space Group of P21221 (pdb code 7v8o). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Crystal Structure of Cyclohexanone Monooxygenase From T. Municipale Mutant L437T Complexed with Nadp+ and Fad in Space Group of P21221, PDB code: 7v8o:

Sodium binding site 1 out of 1 in 7v8o

Go back to Sodium Binding Sites List in 7v8o
Sodium binding site 1 out of 1 in the Crystal Structure of Cyclohexanone Monooxygenase From T. Municipale Mutant L437T Complexed with Nadp+ and Fad in Space Group of P21221


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of Cyclohexanone Monooxygenase From T. Municipale Mutant L437T Complexed with Nadp+ and Fad in Space Group of P21221 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na605

b:41.8
occ:1.00
 OE2 B:GLU252 2.8 30.1 1.0
O B:PHE250 2.9 26.7 1.0
N B:PHE248 3.5 19.8 1.0
CB B:SER244 3.6 18.6 1.0
CD B:GLU252 3.7 30.3 1.0
N B:GLY249 3.7 22.7 1.0
N B:ALA247 3.7 18.9 1.0
OG B:SER244 3.8 18.1 1.0
N B:PHE250 3.9 26.6 1.0
CG2 B:VAL246 3.9 17.9 1.0
CG B:GLU252 3.9 29.6 1.0
C B:PHE250 4.0 27.8 1.0
CE1 B:PHE250 4.1 24.1 1.0
CD1 B:PHE250 4.1 24.7 1.0
CA B:ALA247 4.1 19.0 1.0
C B:ALA247 4.1 19.1 1.0
CA B:PHE248 4.3 20.7 1.0
CZ B:PHE250 4.3 24.5 1.0
CG B:PHE250 4.3 25.6 1.0
C B:PHE248 4.3 21.7 1.0
NE2 B:GLN240 4.4 23.4 1.0
CA B:PHE250 4.5 26.8 1.0
CD2 B:PHE250 4.5 25.1 1.0
CE2 B:PHE250 4.5 25.0 1.0
CB B:PHE248 4.5 20.9 1.0
CA B:GLY249 4.6 24.6 1.0
C B:GLY249 4.6 26.2 1.0
OE1 B:GLN240 4.6 23.6 1.0
C B:VAL246 4.7 18.5 1.0
OE1 B:GLU252 4.8 31.6 1.0
N B:VAL246 4.9 18.6 1.0
CA B:SER244 5.0 19.3 1.0
CB B:GLU252 5.0 28.9 1.0
CD B:GLN240 5.0 23.7 1.0
CB B:PHE250 5.0 26.3 1.0
N B:GLU252 5.0 30.2 1.0

Reference:

Y.J.Dong, T.Li, S.Q.Zhang, J.Sanchis, H.Yin, J.Ren, X.Sheng, G.Y.Li, M.T.Reetz. Biocatalytic Baeyer-Villiger Reactions: Uncovering the Source of Regioselectivity at Each Evolutionary Stage of A Mutant with Scrutiny of Fleeting Chiral Intermediates. Acs Catalysis V. 12 3669 2022.
ISSN: ESSN 2155-5435
DOI: 10.1021/ACSCATAL.2C00415
Page generated: Wed Oct 9 09:17:32 2024

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