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Potassium in PDB 4ks0: Pyruvate Kinase (Pyk) From Trypanosoma Cruzi in the Presence of Magnesium, Oxalate and F26BP

Enzymatic activity of Pyruvate Kinase (Pyk) From Trypanosoma Cruzi in the Presence of Magnesium, Oxalate and F26BP

All present enzymatic activity of Pyruvate Kinase (Pyk) From Trypanosoma Cruzi in the Presence of Magnesium, Oxalate and F26BP:
2.7.1.40;

Protein crystallography data

The structure of Pyruvate Kinase (Pyk) From Trypanosoma Cruzi in the Presence of Magnesium, Oxalate and F26BP, PDB code: 4ks0 was solved by H.P.Morgan, W.Zhong, I.W.Mcnae, P.A.M.Michels, L.A.Fothergill-Gilmore, M.D.Walkinshaw, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 55.87 / 2.80
Space group I 41 2 2
Cell size a, b, c (Å), α, β, γ (°) 173.767, 173.767, 211.855, 90.00, 90.00, 90.00
R / Rfree (%) 17.4 / 21.6

Other elements in 4ks0:

The structure of Pyruvate Kinase (Pyk) From Trypanosoma Cruzi in the Presence of Magnesium, Oxalate and F26BP also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Pyruvate Kinase (Pyk) From Trypanosoma Cruzi in the Presence of Magnesium, Oxalate and F26BP (pdb code 4ks0). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Pyruvate Kinase (Pyk) From Trypanosoma Cruzi in the Presence of Magnesium, Oxalate and F26BP, PDB code: 4ks0:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in 4ks0

Go back to Potassium Binding Sites List in 4ks0
Potassium binding site 1 out of 2 in the Pyruvate Kinase (Pyk) From Trypanosoma Cruzi in the Presence of Magnesium, Oxalate and F26BP


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Pyruvate Kinase (Pyk) From Trypanosoma Cruzi in the Presence of Magnesium, Oxalate and F26BP within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K1002

b:55.4
occ:1.00
O A:THR85 2.7 51.0 1.0
OD1 A:ASP84 2.7 49.3 1.0
OD1 A:ASN52 2.9 49.7 1.0
O A:HOH1223 2.9 60.1 1.0
OG A:SER54 2.9 57.1 1.0
OG A:SER212 3.4 54.1 1.0
CG A:ASP84 3.6 49.6 1.0
C A:THR85 3.7 51.2 1.0
CB A:SER54 3.8 58.3 1.0
NZ A:LYS239 3.9 43.6 1.0
CG A:ASN52 4.0 50.6 1.0
O A:ASP84 4.1 48.3 1.0
OD2 A:ASP84 4.2 53.2 1.0
N A:SER54 4.3 56.4 1.0
C A:ASP84 4.3 47.3 1.0
N A:LYS86 4.3 54.0 1.0
CA A:LYS86 4.3 56.2 1.0
O A:HOH1216 4.3 49.0 1.0
OE2 A:GLU89 4.5 81.2 1.0
N A:THR85 4.5 46.7 1.0
NH2 A:ARG50 4.5 52.0 1.0
CB A:ASP84 4.5 47.6 1.0
CA A:SER54 4.6 57.9 1.0
ND2 A:ASN52 4.6 52.4 1.0
CB A:SER212 4.6 53.0 1.0
O A:LYS86 4.7 57.3 1.0
CA A:THR85 4.7 48.1 1.0
C A:LYS86 4.8 56.4 1.0
N A:PHE53 4.9 54.1 1.0

Potassium binding site 2 out of 2 in 4ks0

Go back to Potassium Binding Sites List in 4ks0
Potassium binding site 2 out of 2 in the Pyruvate Kinase (Pyk) From Trypanosoma Cruzi in the Presence of Magnesium, Oxalate and F26BP


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Pyruvate Kinase (Pyk) From Trypanosoma Cruzi in the Presence of Magnesium, Oxalate and F26BP within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K1002

b:52.1
occ:1.00
O B:HOH1221 2.7 46.8 1.0
OD1 B:ASP84 2.7 48.6 1.0
O B:THR85 2.8 46.2 1.0
OD1 B:ASN52 2.8 48.8 1.0
O B:HOH1179 3.0 25.2 1.0
OG B:SER54 3.1 49.6 1.0
CG B:ASN52 3.7 48.4 1.0
C B:THR85 3.8 46.1 1.0
CG B:ASP84 3.8 47.5 1.0
OG B:SER212 3.8 45.4 1.0
CB B:SER54 3.8 51.0 1.0
O B:ASP84 3.9 45.6 1.0
NZ B:LYS239 4.1 36.1 1.0
ND2 B:ASN52 4.1 50.1 1.0
NH2 B:ARG50 4.2 41.6 1.0
O B:HOH1216 4.2 41.8 1.0
N B:SER54 4.2 50.0 1.0
C B:ASP84 4.2 44.8 1.0
CA B:LYS86 4.3 51.1 1.0
N B:LYS86 4.4 48.6 1.0
O B:LYS86 4.5 55.1 1.0
CB B:ASP84 4.5 46.2 1.0
N B:THR85 4.5 43.9 1.0
OD2 B:ASP84 4.6 47.0 1.0
CA B:SER54 4.6 50.8 1.0
C B:LYS86 4.7 52.7 1.0
N B:PHE53 4.8 47.9 1.0
CA B:THR85 4.8 44.4 1.0
CB B:ASN52 4.9 46.1 1.0
OE2 B:GLU89 4.9 58.4 1.0
CA B:ASN52 5.0 46.5 1.0
CB B:SER212 5.0 44.8 1.0

Reference:

H.P.Morgan, W.Zhong, I.W.Mcnae, P.A.M.Michels, L.A.Fothergill-Gilmore, M.D.Walkinshaw. Structures of Pyruvate Kinases Display Evolutionarily Divergent Allosteric Strategies. R Soc Open Sci. 2014.
ISSN: ESSN 2054-5703
DOI: 10.1098/RSOS.140120
Page generated: Sun Dec 13 23:38:53 2020

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