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Sodium in PDB 2pu7: Crystal Structure of S112A/H265A Double Mutant of A C-C Hydrolase, Bphd, From Burkholderia Xenovorans LB400

Protein crystallography data

The structure of Crystal Structure of S112A/H265A Double Mutant of A C-C Hydrolase, Bphd, From Burkholderia Xenovorans LB400, PDB code: 2pu7 was solved by S.Bhowmik, J.T.Bolin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 82.20 / 2.07
Space group I 41 2 2
Cell size a, b, c (Å), α, β, γ (°) 116.361, 116.361, 87.942, 90.00, 90.00, 90.00
R / Rfree (%) 17.8 / 25.8

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of S112A/H265A Double Mutant of A C-C Hydrolase, Bphd, From Burkholderia Xenovorans LB400 (pdb code 2pu7). 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 S112A/H265A Double Mutant of A C-C Hydrolase, Bphd, From Burkholderia Xenovorans LB400, PDB code: 2pu7:

Sodium binding site 1 out of 1 in 2pu7

Go back to Sodium Binding Sites List in 2pu7
Sodium binding site 1 out of 1 in the Crystal Structure of S112A/H265A Double Mutant of A C-C Hydrolase, Bphd, From Burkholderia Xenovorans LB400


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 S112A/H265A Double Mutant of A C-C Hydrolase, Bphd, From Burkholderia Xenovorans LB400 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na287

b:30.5
occ:1.00
O A:HOH361 2.1 23.7 1.0
O A:HOH362 2.2 32.1 1.0
O9 A:MLI288 2.4 31.1 1.0
O7 A:MLI288 2.5 27.5 1.0
C3 A:MLI288 3.2 22.3 1.0
C2 A:MLI288 3.3 37.7 1.0
C1 A:MLI288 3.5 22.4 1.0
O A:SER180 4.2 47.7 1.0
O8 A:MLI288 4.3 33.5 1.0
O6 A:MLI288 4.5 24.0 1.0
CB A:SER180 4.7 39.0 1.0

Reference:

G.P.Horsman, S.Bhowmik, S.Y.Seah, P.Kumar, J.T.Bolin, L.D.Eltis. The Tautomeric Half-Reaction of Bphd, A C-C Bond Hydrolase: Kinetic and Structural Evidence Supporting A Key Role For Histidine 265 of the Catalytic Triad. J.Biol.Chem. V. 282 19894 2007.
ISSN: ISSN 0021-9258
PubMed: 17442675
DOI: 10.1074/JBC.M702237200
Page generated: Mon Oct 7 03:44:18 2024

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