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Potassium in PDB 1lvg: Crystal Structure of Mouse Guanylate Kinase in Complex with Gmp and Adp

Enzymatic activity of Crystal Structure of Mouse Guanylate Kinase in Complex with Gmp and Adp

All present enzymatic activity of Crystal Structure of Mouse Guanylate Kinase in Complex with Gmp and Adp:
2.7.4.8;

Protein crystallography data

The structure of Crystal Structure of Mouse Guanylate Kinase in Complex with Gmp and Adp, PDB code: 1lvg was solved by N.Sekulic, L.Shuvalova, O.Spangenberg, M.Konrad, A.Lavie, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.10
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 67.241, 67.241, 108.696, 90.00, 90.00, 90.00
R / Rfree (%) 18.8 / 23.1

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of Mouse Guanylate Kinase in Complex with Gmp and Adp (pdb code 1lvg). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Crystal Structure of Mouse Guanylate Kinase in Complex with Gmp and Adp, PDB code: 1lvg:

Potassium binding site 1 out of 1 in 1lvg

Go back to Potassium Binding Sites List in 1lvg
Potassium binding site 1 out of 1 in the Crystal Structure of Mouse Guanylate Kinase in Complex with Gmp and Adp


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structure of Mouse Guanylate Kinase in Complex with Gmp and Adp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K1203

b:22.5
occ:1.00
O A:ASP101 2.6 14.7 1.0
N7 A:5GP1202 2.8 17.8 1.0
O A:HOH1248 2.8 20.2 1.0
O A:HOH1207 2.8 16.1 1.0
O A:HOH1214 2.9 17.8 1.0
OG A:SER37 2.9 19.5 1.0
C8 A:5GP1202 3.3 21.0 1.0
CB A:SER37 3.5 19.5 1.0
C A:ASP101 3.7 16.4 1.0
C5 A:5GP1202 3.8 18.8 1.0
CB A:ASP101 3.9 21.0 1.0
CE1 A:TYR53 4.0 19.2 1.0
CA A:ASP101 4.2 18.3 1.0
O A:HOH1205 4.2 19.1 1.0
N A:ASP101 4.2 18.0 1.0
OH A:TYR53 4.3 19.8 1.0
CG A:ASP101 4.3 26.0 1.0
N9 A:5GP1202 4.4 22.0 1.0
CZ A:TYR53 4.4 18.8 1.0
CZ A:PHE34 4.4 17.8 1.0
C6 A:5GP1202 4.5 17.9 1.0
O6 A:5GP1202 4.5 18.6 1.0
O A:SER35 4.5 16.5 1.0
N A:SER37 4.5 17.3 1.0
C4 A:5GP1202 4.6 19.4 1.0
CA A:SER37 4.7 18.5 1.0
OD1 A:ASP101 4.7 25.7 1.0
CD1 A:TYR53 4.7 16.9 1.0
OD2 A:ASP101 4.8 27.5 1.0
O A:HOH1219 4.8 16.5 1.0
N A:VAL102 4.8 16.5 1.0
CE1 A:PHE34 4.9 20.0 1.0
CG1 A:VAL102 5.0 14.1 1.0

Reference:

N.Sekulic, L.Shuvalova, O.Spangenberg, M.Konrad, A.Lavie. Structural Characterization of the Closed Conformation of Mouse Guanylate Kinase. J.Biol.Chem. V. 277 30236 2002.
ISSN: ISSN 0021-9258
PubMed: 12036965
DOI: 10.1074/JBC.M204668200
Page generated: Mon Aug 12 04:52:37 2024

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