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Potassium in PDB 4msw: Y78 Ester Mutant of Kcsa in High K+

Protein crystallography data

The structure of Y78 Ester Mutant of Kcsa in High K+, PDB code: 4msw was solved by K.Matulef, F.I.Valiyaveetil, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.42 / 2.06
Space group I 4
Cell size a, b, c (Å), α, β, γ (°) 154.530, 154.530, 75.780, 90.00, 90.00, 90.00
R / Rfree (%) 19.6 / 22.9

Potassium Binding Sites:

The binding sites of Potassium atom in the Y78 Ester Mutant of Kcsa in High K+ (pdb code 4msw). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 6 binding sites of Potassium where determined in the Y78 Ester Mutant of Kcsa in High K+, PDB code: 4msw:
Jump to Potassium binding site number: 1; 2; 3; 4; 5; 6;

Potassium binding site 1 out of 6 in 4msw

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Potassium binding site 1 out of 6 in the Y78 Ester Mutant of Kcsa in High K+


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Y78 Ester Mutant of Kcsa in High K+ within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K1002

b:30.0
occ:0.25
O1 C:TYF78 2.9 10.2 1.0
O C:GLY77 2.9 15.7 1.0
C1 C:TYF78 3.5 17.7 1.0
C C:GLY77 4.0 21.4 1.0
C2 C:TYF78 4.1 19.2 1.0
N C:GLY79 4.3 15.8 1.0
O4 C:TYF78 4.5 13.6 1.0
CA C:GLY79 4.6 17.5 1.0
K C:K1006 4.8 30.0 0.2
O C:VAL76 5.0 11.5 1.0

Potassium binding site 2 out of 6 in 4msw

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Potassium binding site 2 out of 6 in the Y78 Ester Mutant of Kcsa in High K+


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Y78 Ester Mutant of Kcsa in High K+ within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K1003

b:30.0
occ:0.25
O C:VAL76 2.9 11.5 1.0
O C:THR75 3.0 11.3 1.0
C C:VAL76 3.6 17.5 1.0
K C:K1004 3.6 30.0 0.2
C C:THR75 4.1 21.6 1.0
CA C:VAL76 4.2 13.6 1.0
N C:GLY77 4.4 18.9 1.0
O C:GLY77 4.5 15.7 1.0
CA C:GLY77 4.7 17.1 1.0
N C:VAL76 4.7 17.4 1.0
C C:GLY77 4.8 21.4 1.0

Potassium binding site 3 out of 6 in 4msw

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Potassium binding site 3 out of 6 in the Y78 Ester Mutant of Kcsa in High K+


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of Y78 Ester Mutant of Kcsa in High K+ within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K1004

b:30.0
occ:0.25
OG1 C:THR75 2.8 14.6 1.0
O C:THR75 2.9 11.3 1.0
CB C:THR75 3.5 14.3 1.0
K C:K1003 3.6 30.0 0.2
C C:THR75 3.7 21.6 1.0
CA C:THR75 4.3 17.8 1.0
N C:VAL76 4.6 17.4 1.0
CG2 C:THR75 4.8 15.9 1.0
CA C:VAL76 4.9 13.6 1.0
O C:THR74 4.9 14.1 1.0

Potassium binding site 4 out of 6 in 4msw

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Potassium binding site 4 out of 6 in the Y78 Ester Mutant of Kcsa in High K+


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 4 of Y78 Ester Mutant of Kcsa in High K+ within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K1005

b:30.0
occ:0.25
O C:HOH1132 3.2 32.1 1.0
O C:HOH1133 3.2 30.1 1.0

Potassium binding site 5 out of 6 in 4msw

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Potassium binding site 5 out of 6 in the Y78 Ester Mutant of Kcsa in High K+


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 5 of Y78 Ester Mutant of Kcsa in High K+ within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K1006

b:30.0
occ:0.25
K C:K1007 2.9 30.0 0.2
O C:HOH1131 3.5 38.2 1.0
O1 C:TYF78 4.1 10.2 1.0
K C:K1002 4.8 30.0 0.2
O C:GLY79 4.9 15.6 1.0

Potassium binding site 6 out of 6 in 4msw

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Potassium binding site 6 out of 6 in the Y78 Ester Mutant of Kcsa in High K+


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 6 of Y78 Ester Mutant of Kcsa in High K+ within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K1007

b:30.0
occ:0.25
K C:K1006 2.9 30.0 0.2
O C:HOH1131 3.3 38.2 1.0

Reference:

K.Matulef, A.G.Komarov, C.A.Costantino, F.I.Valiyaveetil. Using Protein Backbone Mutagenesis to Dissect the Link Between Ion Occupancy and C-Type Inactivation in K+ Channels. Proc.Natl.Acad.Sci.Usa V. 110 17886 2013.
ISSN: ISSN 0027-8424
PubMed: 24128761
DOI: 10.1073/PNAS.1314356110
Page generated: Sun Dec 13 23:45:44 2020

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