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Potassium in PDB 2bwg: Structure of Human Guanosine Monophosphate Reductase GMPR1 in Complex with Gmp

Enzymatic activity of Structure of Human Guanosine Monophosphate Reductase GMPR1 in Complex with Gmp

All present enzymatic activity of Structure of Human Guanosine Monophosphate Reductase GMPR1 in Complex with Gmp:
1.7.1.7;

Protein crystallography data

The structure of Structure of Human Guanosine Monophosphate Reductase GMPR1 in Complex with Gmp, PDB code: 2bwg was solved by G.Bunkoczi, A.Haroniti, S.Ng, F.Von Delft, O.Gileadi, U.Oppermann, C.Arrowsmith, A.Edwards, M.Sundstrom, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.00 / 2.40
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 55.312, 114.418, 115.129, 90.00, 102.74, 90.00
R / Rfree (%) 19.6 / 24.5

Potassium Binding Sites:

The binding sites of Potassium atom in the Structure of Human Guanosine Monophosphate Reductase GMPR1 in Complex with Gmp (pdb code 2bwg). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 4 binding sites of Potassium where determined in the Structure of Human Guanosine Monophosphate Reductase GMPR1 in Complex with Gmp, PDB code: 2bwg:
Jump to Potassium binding site number: 1; 2; 3; 4;

Potassium binding site 1 out of 4 in 2bwg

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Potassium binding site 1 out of 4 in the Structure of Human Guanosine Monophosphate Reductase GMPR1 in Complex with Gmp


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Structure of Human Guanosine Monophosphate Reductase GMPR1 in Complex with Gmp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K1339

b:24.3
occ:1.00
O A:GLY181 2.5 19.8 1.0
O A:GLY183 2.8 11.9 1.0
O A:CYS186 3.1 16.9 1.0
O A:HOH2036 3.2 18.3 1.0
NH2 A:ARG189 3.2 26.4 1.0
C A:GLY181 3.7 20.0 1.0
CZ A:ARG189 3.7 30.0 1.0
C A:PRO182 3.7 18.5 1.0
O A:PRO182 3.8 19.9 1.0
C A:GLY183 3.8 13.8 1.0
C A:CYS186 3.9 14.2 1.0
N A:GLY183 4.0 16.5 1.0
O A:HOH2012 4.1 19.8 1.0
CA A:PRO182 4.1 18.8 1.0
CB A:CYS186 4.1 12.3 1.0
NE A:ARG189 4.1 30.1 1.0
NH1 A:ARG189 4.3 28.6 1.0
N A:PRO182 4.3 19.4 1.0
CA A:CYS186 4.3 12.9 1.0
N A:CYS186 4.4 13.4 1.0
CA A:GLY183 4.4 16.1 1.0
O A:SER184 4.5 12.7 1.0
SG A:CYS186 4.7 15.3 1.0
C A:SER184 4.7 13.7 1.0
N A:SER184 4.8 14.8 1.0
CA A:GLY181 4.8 20.0 1.0
N A:THR187 4.9 13.3 1.0
CA A:SER184 4.9 14.4 1.0

Potassium binding site 2 out of 4 in 2bwg

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Potassium binding site 2 out of 4 in the Structure of Human Guanosine Monophosphate Reductase GMPR1 in Complex with Gmp


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Structure of Human Guanosine Monophosphate Reductase GMPR1 in Complex with Gmp within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K1338

b:26.2
occ:1.00
O B:GLY183 2.8 12.0 1.0
O B:CYS186 2.8 17.0 1.0
O B:GLY181 3.0 19.4 1.0
O B:HOH2027 3.5 11.8 1.0
C B:CYS186 3.8 14.3 1.0
O B:HOH2011 3.8 11.4 1.0
C B:GLY183 3.9 13.9 1.0
NH2 B:ARG189 4.1 26.8 1.0
O B:PRO182 4.1 19.3 1.0
C B:PRO182 4.1 18.3 1.0
O B:SER184 4.2 12.5 1.0
C B:GLY181 4.2 20.2 1.0
CB B:CYS186 4.4 13.3 1.0
N B:CYS186 4.4 13.2 1.0
N B:GLY183 4.4 16.5 1.0
CA B:CYS186 4.4 12.7 1.0
C B:SER184 4.5 13.8 1.0
CZ B:ARG189 4.6 28.0 1.0
CA B:PRO182 4.6 18.7 1.0
CA B:GLY183 4.7 16.4 1.0
N B:SER184 4.8 14.3 1.0
CA B:SER184 4.8 14.4 1.0
N B:THR187 4.8 13.6 1.0
NE B:ARG189 4.8 25.6 1.0
N B:PRO182 4.9 19.4 1.0

Potassium binding site 3 out of 4 in 2bwg

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Potassium binding site 3 out of 4 in the Structure of Human Guanosine Monophosphate Reductase GMPR1 in Complex with Gmp


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of Structure of Human Guanosine Monophosphate Reductase GMPR1 in Complex with Gmp within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K1338

b:31.2
occ:1.00
O C:CYS186 2.8 16.8 1.0
O C:GLY183 2.8 12.3 1.0
O C:GLY181 2.9 19.9 1.0
NH2 C:ARG189 3.5 26.5 1.0
O C:HOH2034 3.8 13.8 1.0
C C:CYS186 3.8 14.1 1.0
C C:GLY183 4.0 14.0 1.0
O C:PRO182 4.0 19.6 1.0
C C:PRO182 4.1 18.6 1.0
CZ C:ARG189 4.2 27.5 1.0
C C:GLY181 4.2 20.2 1.0
O C:SER184 4.2 12.8 1.0
CB C:CYS186 4.4 13.7 1.0
N C:GLY183 4.4 16.9 1.0
N C:CYS186 4.4 13.8 1.0
CA C:CYS186 4.5 13.0 1.0
C C:SER184 4.5 13.8 1.0
CA C:PRO182 4.6 19.0 1.0
NE C:ARG189 4.7 26.7 1.0
NH1 C:ARG189 4.7 31.3 1.0
CA C:GLY183 4.8 15.8 1.0
SG C:CYS186 4.8 18.6 1.0
N C:THR187 4.8 13.8 1.0
N C:SER184 4.8 14.7 1.0
N C:PRO182 4.8 19.3 1.0
CA C:SER184 4.9 14.4 1.0

Potassium binding site 4 out of 4 in 2bwg

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Potassium binding site 4 out of 4 in the Structure of Human Guanosine Monophosphate Reductase GMPR1 in Complex with Gmp


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 4 of Structure of Human Guanosine Monophosphate Reductase GMPR1 in Complex with Gmp within 5.0Å range:
probe atom residue distance (Å) B Occ
D:K1338

b:22.1
occ:1.00
O D:GLY183 2.8 11.9 1.0
O D:GLY181 2.8 19.9 1.0
O D:CYS186 3.0 16.8 1.0
NH2 D:ARG189 3.5 30.2 1.0
O D:HOH2011 3.6 24.3 1.0
O D:HOH2026 3.7 14.1 1.0
C D:GLY183 3.8 13.9 1.0
C D:CYS186 3.9 14.3 1.0
C D:PRO182 4.0 18.4 1.0
C D:GLY181 4.0 20.2 1.0
O D:PRO182 4.0 19.4 1.0
CZ D:ARG189 4.1 28.4 1.0
N D:GLY183 4.2 16.7 1.0
O D:SER184 4.3 12.9 1.0
CB D:CYS186 4.4 13.1 1.0
CA D:PRO182 4.4 18.9 1.0
N D:CYS186 4.5 13.4 1.0
CA D:CYS186 4.5 12.9 1.0
C D:SER184 4.6 13.7 1.0
CA D:GLY183 4.6 16.1 1.0
N D:PRO182 4.7 19.4 1.0
NE D:ARG189 4.7 27.0 1.0
NH1 D:ARG189 4.7 29.3 1.0
N D:SER184 4.7 14.5 1.0
CA D:SER184 4.8 14.4 1.0
N D:THR187 4.9 13.6 1.0
SG D:CYS186 4.9 15.2 1.0

Reference:

G.Bunkoczi, A.Haroniti, S.Ng, F.Von Delft, O.Gileadi, U.Oppermann, C.Arrowsmith, A.Edwards, M.Sundstrom. Structure of Human Guanosine Monophosphate Reductase GMPR1 in Complex with Gmp To Be Published.
Page generated: Mon Aug 12 06:08:49 2024

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