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Sodium in PDB 1x9j: Structure of Butyrate Kinase 2 Reveals Both Open- and Citrate-Induced Closed Conformations: Implications For Substrate-Induced Fit Conformational Changes

Enzymatic activity of Structure of Butyrate Kinase 2 Reveals Both Open- and Citrate-Induced Closed Conformations: Implications For Substrate-Induced Fit Conformational Changes

All present enzymatic activity of Structure of Butyrate Kinase 2 Reveals Both Open- and Citrate-Induced Closed Conformations: Implications For Substrate-Induced Fit Conformational Changes:
2.7.2.7;

Protein crystallography data

The structure of Structure of Butyrate Kinase 2 Reveals Both Open- and Citrate-Induced Closed Conformations: Implications For Substrate-Induced Fit Conformational Changes, PDB code: 1x9j was solved by J.S.Diao, D.A.Sanders, M.S.Hasson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 91.48 / 3.00
Space group P 43
Cell size a, b, c (Å), α, β, γ (°) 193.680, 193.680, 122.932, 90.00, 90.00, 90.00
R / Rfree (%) 26.1 / 28.4

Sodium Binding Sites:

The binding sites of Sodium atom in the Structure of Butyrate Kinase 2 Reveals Both Open- and Citrate-Induced Closed Conformations: Implications For Substrate-Induced Fit Conformational Changes (pdb code 1x9j). 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 Structure of Butyrate Kinase 2 Reveals Both Open- and Citrate-Induced Closed Conformations: Implications For Substrate-Induced Fit Conformational Changes, PDB code: 1x9j:

Sodium binding site 1 out of 1 in 1x9j

Go back to Sodium Binding Sites List in 1x9j
Sodium binding site 1 out of 1 in the Structure of Butyrate Kinase 2 Reveals Both Open- and Citrate-Induced Closed Conformations: Implications For Substrate-Induced Fit Conformational Changes


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Structure of Butyrate Kinase 2 Reveals Both Open- and Citrate-Induced Closed Conformations: Implications For Substrate-Induced Fit Conformational Changes within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Na380

b:24.0
occ:1.00
O D:TYR63 2.4 37.4 1.0
O D:VAL58 2.5 28.1 1.0
N D:TYR63 3.2 30.0 1.0
OG1 D:THR61 3.4 32.1 1.0
C D:TYR63 3.5 34.9 1.0
C D:VAL58 3.6 29.6 1.0
O D:GLU59 3.7 31.4 1.0
C D:THR61 3.7 29.3 1.0
O D:THR61 3.7 31.4 1.0
N D:GLY62 3.7 27.4 1.0
CA D:GLU59 3.8 30.4 1.0
C D:GLY62 3.9 28.8 1.0
C D:GLU59 3.9 31.2 1.0
CA D:GLY62 3.9 27.1 1.0
CA D:TYR63 3.9 32.6 1.0
N D:THR61 4.1 33.0 1.0
N D:GLU59 4.1 29.5 1.0
CG1 D:VAL58 4.3 29.0 1.0
CA D:THR61 4.3 30.8 1.0
CB D:THR61 4.5 29.8 1.0
N D:SER64 4.6 35.7 1.0
CA D:VAL58 4.7 28.8 1.0
N D:GLU60 4.8 33.4 1.0
CB D:TYR63 4.8 33.8 1.0
O D:GLY62 4.8 28.7 1.0

Reference:

J.S.Diao, S.Bhattacharyya, Y.L.D.Ma, D.A.Sanders, M.S.Hasson. Structure of Butyrate Kinase 2 Reveals Both Open and Closed Conformations of the Two Domains: Implications For Substrate-Induced Changes To Be Published.
Page generated: Mon Oct 7 00:31:51 2024

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