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Potassium in PDB 2a0l: Crystal Structure of Kvap-33H1 Fv Complex

Protein crystallography data

The structure of Crystal Structure of Kvap-33H1 Fv Complex, PDB code: 2a0l was solved by S.Y.Lee, A.Lee, J.Chen, R.Mackinnon, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 57.89 / 3.90
Space group P 42 2 2
Cell size a, b, c (Å), α, β, γ (°) 136.362, 136.362, 191.812, 90.00, 90.00, 90.00
R / Rfree (%) 35.8 / 39.2

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of Kvap-33H1 Fv Complex (pdb code 2a0l). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 4 binding sites of Potassium where determined in the Crystal Structure of Kvap-33H1 Fv Complex, PDB code: 2a0l:
Jump to Potassium binding site number: 1; 2; 3; 4;

Potassium binding site 1 out of 4 in 2a0l

Go back to Potassium Binding Sites List in 2a0l
Potassium binding site 1 out of 4 in the Crystal Structure of Kvap-33H1 Fv Complex


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 Kvap-33H1 Fv Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K1

b:0.5
occ:0.50
K A:K2 3.4 0.5 0.5
O B:TYR199 3.5 0.9 1.0
O A:TYR199 3.6 0.7 1.0
C B:TYR199 3.7 0.9 1.0
C A:TYR199 3.8 0.7 1.0
CA B:TYR199 4.0 0.9 1.0
O A:GLY198 4.0 0.2 1.0
O B:GLY198 4.0 0.4 1.0
CA A:TYR199 4.0 0.7 1.0
N B:GLY200 4.3 0.7 1.0
N A:GLY200 4.4 0.6 1.0
C B:GLY198 4.7 0.4 1.0
C A:GLY198 4.7 0.2 1.0
N B:TYR199 4.8 0.9 1.0
CA B:GLY200 4.8 0.7 1.0
N A:TYR199 4.8 0.7 1.0
CA A:GLY200 4.9 0.6 1.0

Potassium binding site 2 out of 4 in 2a0l

Go back to Potassium Binding Sites List in 2a0l
Potassium binding site 2 out of 4 in the Crystal Structure of Kvap-33H1 Fv Complex


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Crystal Structure of Kvap-33H1 Fv Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K2

b:0.5
occ:0.50
O B:GLY198 3.1 0.4 1.0
O A:GLY198 3.1 0.2 1.0
K A:K3 3.2 0.5 0.5
O B:VAL197 3.2 0.6 1.0
O A:VAL197 3.2 0.9 1.0
K B:K1 3.4 0.5 0.5
C B:GLY198 4.1 0.4 1.0
C A:GLY198 4.2 0.2 1.0
C B:VAL197 4.4 0.6 1.0
C A:VAL197 4.4 0.9 1.0
CA B:GLY198 4.7 0.4 1.0
CA A:GLY198 4.8 0.2 1.0

Potassium binding site 3 out of 4 in 2a0l

Go back to Potassium Binding Sites List in 2a0l
Potassium binding site 3 out of 4 in the Crystal Structure of Kvap-33H1 Fv Complex


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of Crystal Structure of Kvap-33H1 Fv Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K3

b:0.5
occ:0.50
O B:THR196 3.1 0.5 1.0
O A:THR196 3.2 0.4 1.0
K A:K2 3.2 0.5 0.5
O B:VAL197 3.3 0.6 1.0
K B:K4 3.3 0.5 0.5
O A:VAL197 3.4 0.9 1.0
C B:VAL197 4.1 0.6 1.0
C A:VAL197 4.2 0.9 1.0
C B:THR196 4.3 0.5 1.0
C A:THR196 4.3 0.4 1.0
CA B:VAL197 4.4 0.6 1.0
CA A:VAL197 4.5 0.9 1.0
N B:VAL197 4.8 0.6 1.0
O B:GLY198 4.9 0.4 1.0
N A:VAL197 4.9 0.9 1.0

Potassium binding site 4 out of 4 in 2a0l

Go back to Potassium Binding Sites List in 2a0l
Potassium binding site 4 out of 4 in the Crystal Structure of Kvap-33H1 Fv Complex


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 4 of Crystal Structure of Kvap-33H1 Fv Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K4

b:0.5
occ:0.50
O B:THR196 3.1 0.5 1.0
O A:THR196 3.3 0.4 1.0
K A:K3 3.3 0.5 0.5
OG1 B:THR196 3.4 0.7 1.0
OG1 A:THR196 3.5 1.0 1.0
CB B:THR196 3.6 0.7 1.0
CB A:THR196 3.8 1.0 1.0
C B:THR196 4.0 0.5 1.0
C A:THR196 4.2 0.4 1.0
CA B:THR196 4.4 0.5 1.0
CA A:THR196 4.6 0.4 1.0
CG2 B:THR196 4.9 0.7 1.0
CG2 A:THR196 4.9 1.0 1.0

Reference:

S.Y.Lee, A.Lee, J.Chen, R.Mackinnon. Structure of the Kvap Voltage-Dependent K+ Channel and Its Dependence on the Lipid Membrane. Proc.Natl.Acad.Sci.Usa V. 102 15441 2005.
ISSN: ISSN 0027-8424
PubMed: 16223877
DOI: 10.1073/PNAS.0507651102
Page generated: Sun Dec 13 23:08:29 2020

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