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Potassium in PDB 2fpl: Rada Recombinase in Complex with Amp-Pnp and Low Concentration of K+

Protein crystallography data

The structure of Rada Recombinase in Complex with Amp-Pnp and Low Concentration of K+, PDB code: 2fpl 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 / 2.30
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 83.454, 83.454, 106.825, 90.00, 90.00, 120.00
R / Rfree (%) 19.7 / 24.9

Other elements in 2fpl:

The structure of Rada Recombinase in Complex with Amp-Pnp and Low Concentration of K+ 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 Amp-Pnp and Low Concentration of K+ (pdb code 2fpl). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 3 binding sites of Potassium where determined in the Rada Recombinase in Complex with Amp-Pnp and Low Concentration of K+, PDB code: 2fpl:
Jump to Potassium binding site number: 1; 2; 3;

Potassium binding site 1 out of 3 in 2fpl

Go back to Potassium Binding Sites List in 2fpl
Potassium binding site 1 out of 3 in the Rada Recombinase in Complex with Amp-Pnp and Low Concentration of K+


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 Amp-Pnp and Low Concentration of K+ within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K503

b:39.8
occ:1.00
OD2 A:ASP302 2.7 20.9 1.0
O A:ALA282 2.7 20.9 1.0
O A:HOH608 2.9 14.2 1.0
O A:THR283 3.0 18.2 1.0
CG A:ASP302 3.5 21.2 1.0
C A:THR283 3.6 18.0 1.0
CA A:THR283 3.7 18.6 1.0
C A:ALA282 3.8 20.2 1.0
OD1 A:ASP302 3.9 21.0 1.0
N A:THR283 4.2 19.5 1.0
NE A:ARG285 4.5 22.0 1.0
N A:PHE284 4.6 17.6 1.0
N A:SER303 4.7 20.6 1.0
CA A:SER303 4.7 21.1 1.0
CB A:ASP302 4.7 21.0 1.0
C A:SER303 4.8 21.5 1.0
NH2 A:ARG285 4.9 23.4 1.0
C A:ASP302 4.9 20.1 1.0
CD A:PRO304 4.9 20.9 1.0

Potassium binding site 2 out of 3 in 2fpl

Go back to Potassium Binding Sites List in 2fpl
Potassium binding site 2 out of 3 in the Rada Recombinase in Complex with Amp-Pnp and Low Concentration of K+


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Rada Recombinase in Complex with Amp-Pnp and Low Concentration of K+ within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K505

b:38.0
occ:1.00
O A:HOH632 2.7 17.5 1.0
O3' A:ANP401 2.7 20.7 1.0
O2' A:ANP401 2.8 23.3 1.0
C3' A:ANP401 3.4 21.0 1.0
C2' A:ANP401 3.7 21.4 1.0
NH2 A:ARG296 4.0 24.1 1.0
C4' A:ANP401 4.1 21.1 1.0
NZ A:LYS290 4.3 45.6 1.0
CE A:LYS290 4.6 47.5 1.0
C1' A:ANP401 4.9 21.0 1.0
C5' A:ANP401 5.0 20.1 1.0

Potassium binding site 3 out of 3 in 2fpl

Go back to Potassium Binding Sites List in 2fpl
Potassium binding site 3 out of 3 in the Rada Recombinase in Complex with Amp-Pnp and Low Concentration of K+


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of Rada Recombinase in Complex with Amp-Pnp and Low Concentration of K+ within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K506

b:26.4
occ:1.00
O A:THR6 2.6 28.2 1.0
O A:LEU8 2.7 28.0 1.0
O A:HOH720 2.7 44.4 1.0
O A:VAL11 2.8 34.5 1.0
O A:HOH691 3.0 33.8 1.0
C A:THR6 3.6 28.5 1.0
C A:VAL11 3.6 35.9 1.0
N A:VAL11 3.7 37.8 1.0
C A:LEU8 3.7 28.8 1.0
CA A:VAL11 4.0 36.6 1.0
CA A:THR6 4.2 29.2 1.0
CB A:VAL11 4.3 36.4 1.0
N A:GLY10 4.3 35.4 1.0
C A:ASP7 4.3 30.2 1.0
N A:LEU8 4.4 29.4 1.0
CA A:PRO9 4.4 31.3 1.0
N A:PRO9 4.5 30.4 1.0
O A:ASP7 4.5 31.2 1.0
O A:HOH699 4.5 47.2 1.0
N A:ASP7 4.5 28.6 1.0
C A:PRO9 4.6 33.4 1.0
CA A:LEU8 4.6 28.1 1.0
CB A:THR6 4.7 30.1 1.0
N A:GLY12 4.7 36.6 1.0
CA A:ASP7 4.8 30.5 1.0
C A:GLY10 4.8 37.6 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: Mon Aug 12 06:23:14 2024

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