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Potassium in PDB 2fpk: Rada Recombinase in Complex with Adp

Protein crystallography data

The structure of Rada Recombinase in Complex with Adp, PDB code: 2fpk was solved by Y.Wu, X.Qian, Y.He, I.A.Moya, Y.Luo, 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 61
Cell size a, b, c (Å), α, β, γ (°) 83.986, 83.986, 106.367, 90.00, 90.00, 120.00
R / Rfree (%) 23 / 25.7

Other elements in 2fpk:

The structure of Rada Recombinase in Complex with Adp also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Rada Recombinase in Complex with Adp (pdb code 2fpk). 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 Rada Recombinase in Complex with Adp, PDB code: 2fpk:

Potassium binding site 1 out of 1 in 2fpk

Go back to Potassium Binding Sites List in 2fpk
Potassium binding site 1 out of 1 in the Rada Recombinase in Complex with Adp


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Rada Recombinase in Complex with Adp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K506

b:30.6
occ:1.00
O A:THR6 2.5 26.8 1.0
O A:VAL11 2.7 34.7 1.0
O A:LEU8 2.7 29.7 1.0
O A:HOH635 2.8 42.4 1.0
C A:THR6 3.5 27.4 1.0
C A:VAL11 3.6 34.2 1.0
N A:VAL11 3.6 34.0 1.0
C A:LEU8 3.7 30.4 1.0
N A:GLY10 4.0 33.5 1.0
CA A:VAL11 4.0 33.4 1.0
CA A:THR6 4.1 27.4 1.0
C A:ASP7 4.2 30.2 1.0
C A:GLY10 4.3 34.9 1.0
N A:LEU8 4.3 28.9 1.0
O A:ASP7 4.3 30.9 1.0
N A:PRO9 4.4 30.2 1.0
CA A:PRO9 4.4 31.2 1.0
CB A:VAL11 4.4 32.2 1.0
C A:PRO9 4.4 32.1 1.0
N A:ASP7 4.5 29.1 1.0
CA A:LEU8 4.6 29.9 1.0
CB A:THR6 4.6 28.6 1.0
CA A:GLY10 4.7 33.9 1.0
N A:GLY12 4.7 35.5 1.0
CA A:ASP7 4.7 30.4 1.0

Reference:

X.Qian, Y.Wu, Y.He, I.A.Moya, Y.Luo. Crystal Structure of Methanococcus Voltae Rada in Complex with Adp: Hydrolysis-Induced Conformational Change Biochemistry V. 44 13753 2005.
ISSN: ISSN 0006-2960
PubMed: 16229465
DOI: 10.1021/BI051222I
Page generated: Sun Dec 13 23:09:49 2020

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