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Sodium in PDB 2puj: Crystal Structure of the S112A/H265A Double Mutant of A C-C Hydrolase, Bphd From Burkholderia Xenovorans LB400, in Complex with Its Substrate Hopda

Protein crystallography data

The structure of Crystal Structure of the S112A/H265A Double Mutant of A C-C Hydrolase, Bphd From Burkholderia Xenovorans LB400, in Complex with Its Substrate Hopda, PDB code: 2puj 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) 82.48 / 1.57
Space group I 41 2 2
Cell size a, b, c (Å), α, β, γ (°) 116.805, 116.805, 87.528, 90.00, 90.00, 90.00
R / Rfree (%) 17.5 / 20.2

Sodium Binding Sites:

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

Sodium binding site 1 out of 1 in 2puj

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


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

b:27.4
occ:1.00
O A:HOH340 2.2 43.5 1.0
O A:HOH429 2.3 25.3 1.0
O9 A:MLI288 2.3 30.7 1.0
O7 A:MLI288 2.5 24.8 1.0
C3 A:MLI288 3.2 45.1 1.0
C2 A:MLI288 3.4 28.2 1.0
C1 A:MLI288 3.4 27.9 1.0
O A:HOH358 3.8 37.8 1.0
O A:SER180 3.9 33.3 1.0
O8 A:MLI288 4.3 31.7 1.0
CB A:SER180 4.4 56.9 0.5
CB A:SER180 4.5 18.9 0.5
O6 A:MLI288 4.6 27.8 1.0
CA A:SER180 4.8 28.5 0.5
C A:SER180 4.8 48.3 1.0
CA A:SER180 4.8 23.8 0.5

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: Tue Dec 15 05:54:12 2020

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