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Potassium in PDB 4kcw: Pyruvate Kinase (Pyk) From Trypanosoma Brucei Soaked with Oxalate

Enzymatic activity of Pyruvate Kinase (Pyk) From Trypanosoma Brucei Soaked with Oxalate

All present enzymatic activity of Pyruvate Kinase (Pyk) From Trypanosoma Brucei Soaked with Oxalate:
2.7.1.40;

Protein crystallography data

The structure of Pyruvate Kinase (Pyk) From Trypanosoma Brucei Soaked with Oxalate, PDB code: 4kcw was solved by W.Zhong, H.P.Morgan, 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) 68.44 / 2.50
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 103.880, 108.560, 264.530, 90.00, 90.00, 90.00
R / Rfree (%) 16 / 20.2

Other elements in 4kcw:

The structure of Pyruvate Kinase (Pyk) From Trypanosoma Brucei Soaked with Oxalate 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 Brucei Soaked with Oxalate (pdb code 4kcw). 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 Brucei Soaked with Oxalate, PDB code: 4kcw:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in 4kcw

Go back to Potassium Binding Sites List in 4kcw
Potassium binding site 1 out of 2 in the Pyruvate Kinase (Pyk) From Trypanosoma Brucei Soaked with Oxalate


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 Brucei Soaked with Oxalate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K1002

b:34.2
occ:1.00
OD1 A:ASP84 2.6 28.8 1.0
OD1 A:ASN52 2.7 34.5 1.0
O A:THR85 2.8 35.1 1.0
O A:HOH1172 2.8 34.0 1.0
O A:HOH1186 2.9 30.3 1.0
OG A:SER54 3.0 34.0 1.0
CG A:ASP84 3.6 26.5 1.0
C A:THR85 3.7 32.8 1.0
OG A:SER212 3.7 27.1 1.0
CG A:ASN52 3.8 34.0 1.0
O A:ASP84 3.9 29.1 1.0
NZ A:LYS239 4.0 29.1 1.0
CB A:SER54 4.0 33.0 1.0
NH2 A:ARG50 4.1 27.8 1.0
N A:LYS86 4.1 34.0 1.0
CA A:LYS86 4.2 34.6 1.0
C A:ASP84 4.2 30.6 1.0
N A:SER54 4.2 33.2 1.0
OE1 A:GLU89 4.3 50.0 1.0
ND2 A:ASN52 4.3 26.9 1.0
OD2 A:ASP84 4.4 27.1 1.0
CB A:ASP84 4.4 26.1 1.0
O A:HOH1184 4.5 27.8 1.0
N A:THR85 4.5 30.3 1.0
O A:LYS86 4.6 33.6 1.0
CA A:SER54 4.6 37.1 1.0
CA A:THR85 4.7 31.1 1.0
N A:PHE53 4.7 31.7 1.0
C A:LYS86 4.7 34.0 1.0
CB A:SER212 4.9 27.9 1.0
CB A:ASN52 4.9 32.3 1.0
CA A:ASN52 4.9 31.2 1.0
CA A:ASP84 5.0 28.3 1.0

Potassium binding site 2 out of 2 in 4kcw

Go back to Potassium Binding Sites List in 4kcw
Potassium binding site 2 out of 2 in the Pyruvate Kinase (Pyk) From Trypanosoma Brucei Soaked with Oxalate


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 Brucei Soaked with Oxalate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K1002

b:47.0
occ:1.00
OD1 B:ASN52 2.6 32.3 1.0
OD1 B:ASP84 2.7 32.5 1.0
O B:HOH1101 2.7 26.8 1.0
O B:THR85 2.9 27.9 1.0
O B:HOH1172 3.0 39.6 1.0
OG B:SER54 3.2 50.1 1.0
C B:THR85 3.6 28.9 1.0
CG B:ASP84 3.7 33.8 1.0
CG B:ASN52 3.7 31.8 1.0
O B:ASP84 3.8 28.6 1.0
OG B:SER212 3.8 28.4 1.0
NZ B:LYS239 3.9 25.2 1.0
CB B:SER54 3.9 40.0 1.0
C B:ASP84 4.0 28.0 1.0
NH2 B:ARG50 4.1 27.2 1.0
N B:SER54 4.1 39.3 1.0
N B:LYS86 4.2 34.9 1.0
CA B:LYS86 4.3 35.0 1.0
N B:THR85 4.3 26.6 1.0
CB B:ASP84 4.3 31.1 1.0
ND2 B:ASN52 4.4 30.6 1.0
O B:HOH1198 4.4 40.5 1.0
OD2 B:ASP84 4.5 36.6 1.0
CA B:SER54 4.6 44.0 1.0
CA B:THR85 4.6 28.1 1.0
O B:HOH1171 4.6 28.8 1.0
N B:PHE53 4.6 33.5 1.0
O B:LYS86 4.6 35.5 1.0
CA B:ASN52 4.8 28.5 1.0
C B:LYS86 4.8 33.4 1.0
CA B:ASP84 4.8 28.6 1.0
CB B:ASN52 4.8 28.7 1.0
C B:ASN52 5.0 29.3 1.0

Reference:

W.Zhong, H.P.Morgan, M.W.Nowicki, I.W.Mcnae, M.Yuan, J.Bella, P.A.Michels, L.A.Fothergill-Gilmore, M.D.Walkinshaw. Pyruvate Kinases Have An Intrinsic and Conserved Decarboxylase Activity. Biochem.J. V. 458 301 2014.
ISSN: ISSN 0264-6021
PubMed: 24328825
DOI: 10.1042/BJ20130790
Page generated: Mon Aug 12 11:11:10 2024

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