Atomistry » Potassium » PDB 4bga-4cn0 » 4cfs
Atomistry »
  Potassium »
    PDB 4bga-4cn0 »
      4cfs »

Potassium in PDB 4cfs: Crystal Structure of the Cofactor-Devoid 1-H-3-Hydroxy-4- Oxoquinaldine 2,4-Dioxygenase (Hod) Catalytically Inactive H251A Variant Complexed with Its Natural Substrate 1-H-3- Hydroxy-4-Oxoquinaldine

Enzymatic activity of Crystal Structure of the Cofactor-Devoid 1-H-3-Hydroxy-4- Oxoquinaldine 2,4-Dioxygenase (Hod) Catalytically Inactive H251A Variant Complexed with Its Natural Substrate 1-H-3- Hydroxy-4-Oxoquinaldine

All present enzymatic activity of Crystal Structure of the Cofactor-Devoid 1-H-3-Hydroxy-4- Oxoquinaldine 2,4-Dioxygenase (Hod) Catalytically Inactive H251A Variant Complexed with Its Natural Substrate 1-H-3- Hydroxy-4-Oxoquinaldine:
1.13.11.48;

Protein crystallography data

The structure of Crystal Structure of the Cofactor-Devoid 1-H-3-Hydroxy-4- Oxoquinaldine 2,4-Dioxygenase (Hod) Catalytically Inactive H251A Variant Complexed with Its Natural Substrate 1-H-3- Hydroxy-4-Oxoquinaldine, PDB code: 4cfs was solved by S.Bui, R.A.Steiner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.45 / 1.94
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 44.730, 166.850, 167.740, 90.00, 90.00, 90.00
R / Rfree (%) 16.287 / 19.841

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of the Cofactor-Devoid 1-H-3-Hydroxy-4- Oxoquinaldine 2,4-Dioxygenase (Hod) Catalytically Inactive H251A Variant Complexed with Its Natural Substrate 1-H-3- Hydroxy-4-Oxoquinaldine (pdb code 4cfs). 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 the Cofactor-Devoid 1-H-3-Hydroxy-4- Oxoquinaldine 2,4-Dioxygenase (Hod) Catalytically Inactive H251A Variant Complexed with Its Natural Substrate 1-H-3- Hydroxy-4-Oxoquinaldine, PDB code: 4cfs:
Jump to Potassium binding site number: 1; 2; 3; 4;

Potassium binding site 1 out of 4 in 4cfs

Go back to Potassium Binding Sites List in 4cfs
Potassium binding site 1 out of 4 in the Crystal Structure of the Cofactor-Devoid 1-H-3-Hydroxy-4- Oxoquinaldine 2,4-Dioxygenase (Hod) Catalytically Inactive H251A Variant Complexed with Its Natural Substrate 1-H-3- Hydroxy-4-Oxoquinaldine


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 the Cofactor-Devoid 1-H-3-Hydroxy-4- Oxoquinaldine 2,4-Dioxygenase (Hod) Catalytically Inactive H251A Variant Complexed with Its Natural Substrate 1-H-3- Hydroxy-4-Oxoquinaldine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K1276

b:34.0
occ:1.00
 O A:ALA235 2.6 39.5 1.0
O A:PHE241 2.6 24.8 1.0
O A:HOH2149 2.6 33.0 1.0
O A:HIS238 3.0 35.3 1.0
O A:HOH2147 3.0 33.8 1.0
O A:HOH2060 3.4 24.3 1.0
C A:ALA235 3.6 37.7 1.0
O A:PRO239 3.6 29.8 1.0
C A:PRO239 3.8 31.3 1.0
CA A:PRO239 3.8 35.0 1.0
C A:PHE241 3.8 25.9 1.0
C A:HIS238 3.9 35.0 1.0
CA A:ALA235 3.9 34.4 1.0
CB A:ALA235 4.0 34.8 1.0
N A:PRO239 4.3 35.3 1.0
N A:PHE241 4.3 28.3 1.0
O D:HOH2112 4.4 39.0 1.0
CA A:PHE241 4.6 25.8 1.0
N A:TRP240 4.6 30.3 1.0
N A:GLU236 4.7 39.4 1.0
N A:SER242 4.8 25.2 1.0
OD2 D:ASP158 4.9 31.7 1.0

Potassium binding site 2 out of 4 in 4cfs

Go back to Potassium Binding Sites List in 4cfs
Potassium binding site 2 out of 4 in the Crystal Structure of the Cofactor-Devoid 1-H-3-Hydroxy-4- Oxoquinaldine 2,4-Dioxygenase (Hod) Catalytically Inactive H251A Variant Complexed with Its Natural Substrate 1-H-3- Hydroxy-4-Oxoquinaldine


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 the Cofactor-Devoid 1-H-3-Hydroxy-4- Oxoquinaldine 2,4-Dioxygenase (Hod) Catalytically Inactive H251A Variant Complexed with Its Natural Substrate 1-H-3- Hydroxy-4-Oxoquinaldine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K1276

b:25.6
occ:1.00
 O B:PHE241 2.5 17.3 1.0
O B:HOH2159 2.6 27.2 1.0
O B:ALA235 2.7 25.9 1.0
O B:HIS238 2.9 29.5 1.0
O B:HOH2050 3.1 29.1 1.0
O B:HOH2154 3.3 27.1 1.0
O B:PRO239 3.6 18.9 1.0
C B:ALA235 3.6 24.6 1.0
C B:PHE241 3.7 18.2 1.0
C B:PRO239 3.8 23.6 1.0
CA B:PRO239 3.9 26.4 1.0
C B:HIS238 3.9 27.7 1.0
CA B:ALA235 3.9 22.6 1.0
CB B:ALA235 4.0 23.1 1.0
N B:PHE241 4.2 19.8 1.0
N B:PRO239 4.3 27.9 1.0
CA B:PHE241 4.4 17.8 1.0
N B:TRP240 4.6 23.1 1.0
N B:SER242 4.7 17.3 1.0
N B:GLU236 4.8 25.7 1.0
CA B:SER242 4.9 16.9 1.0
CB B:PHE241 4.9 19.0 1.0
C B:TRP240 5.0 20.6 1.0

Potassium binding site 3 out of 4 in 4cfs

Go back to Potassium Binding Sites List in 4cfs
Potassium binding site 3 out of 4 in the Crystal Structure of the Cofactor-Devoid 1-H-3-Hydroxy-4- Oxoquinaldine 2,4-Dioxygenase (Hod) Catalytically Inactive H251A Variant Complexed with Its Natural Substrate 1-H-3- Hydroxy-4-Oxoquinaldine


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 the Cofactor-Devoid 1-H-3-Hydroxy-4- Oxoquinaldine 2,4-Dioxygenase (Hod) Catalytically Inactive H251A Variant Complexed with Its Natural Substrate 1-H-3- Hydroxy-4-Oxoquinaldine within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K1276

b:31.6
occ:1.00
 O A:HOH2099 2.3 38.4 1.0
O C:PHE241 2.6 25.2 1.0
O C:HOH2116 2.8 22.0 1.0
O C:ALA235 2.8 32.0 1.0
O C:HOH2117 2.9 29.0 1.0
O C:HIS238 3.2 36.3 1.0
O A:HOH2031 3.3 31.9 1.0
O C:PRO239 3.5 27.9 1.0
C C:ALA235 3.7 28.1 1.0
C C:PHE241 3.8 27.2 1.0
C C:PRO239 3.8 30.9 1.0
CA C:PRO239 3.9 32.5 1.0
CA C:ALA235 4.1 24.5 1.0
C C:HIS238 4.1 33.5 1.0
CB C:ALA235 4.1 24.1 1.0
N C:PHE241 4.3 26.6 1.0
OD2 A:ASP158 4.3 29.0 1.0
N C:PRO239 4.4 34.1 1.0
O A:HOH2083 4.5 20.3 0.5
CA C:PHE241 4.6 25.2 1.0
N C:TRP240 4.7 28.1 1.0
N C:SER242 4.7 25.9 1.0
CA C:SER242 4.9 26.8 1.0
CB A:ASP158 4.9 26.4 1.0
N C:GLU236 4.9 32.3 1.0

Potassium binding site 4 out of 4 in 4cfs

Go back to Potassium Binding Sites List in 4cfs
Potassium binding site 4 out of 4 in the Crystal Structure of the Cofactor-Devoid 1-H-3-Hydroxy-4- Oxoquinaldine 2,4-Dioxygenase (Hod) Catalytically Inactive H251A Variant Complexed with Its Natural Substrate 1-H-3- Hydroxy-4-Oxoquinaldine


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 the Cofactor-Devoid 1-H-3-Hydroxy-4- Oxoquinaldine 2,4-Dioxygenase (Hod) Catalytically Inactive H251A Variant Complexed with Its Natural Substrate 1-H-3- Hydroxy-4-Oxoquinaldine within 5.0Å range:
probe atom residue distance (Å) B Occ
D:K1276

b:28.6
occ:1.00
 O D:HOH2164 2.5 33.0 1.0
O D:PHE241 2.6 21.2 1.0
O D:ALA235 2.8 26.4 1.0
O D:HOH2166 2.8 48.2 1.0
O D:HOH2161 2.9 29.9 1.0
O D:HIS238 3.0 31.7 1.0
O D:HOH2162 3.2 38.4 1.0
O D:PRO239 3.5 28.1 1.0
C D:ALA235 3.7 26.5 1.0
C D:PRO239 3.7 27.1 1.0
C D:PHE241 3.8 22.8 1.0
CA D:PRO239 3.8 28.4 1.0
C D:HIS238 3.9 28.1 1.0
CA D:ALA235 4.0 25.9 1.0
CB D:ALA235 4.1 24.3 1.0
N D:PHE241 4.3 23.0 1.0
N D:PRO239 4.3 28.2 1.0
O D:HOH2165 4.4 30.0 1.0
CA D:PHE241 4.5 21.8 1.0
N D:TRP240 4.6 26.8 1.0
N D:SER242 4.7 21.9 1.0
N D:GLU236 4.8 29.6 1.0
CA D:SER242 4.9 22.7 1.0

Reference:

A.Hernandez-Ortega, M.G.Quesne, S.Bui, D.P.Heuts, R.A.Steiner, D.J.Heyes, S.P.De Visser, N.S.Scrutton. Origin of the Proton-Transfer Step in the Cofactor-Free 1-H- 3-Hydroxy-4-Oxoquinaldine 2,4- Dioxygenase: Effect of the Basicity of An Active Site His Residue. J.Biol.Chem. V. 289 8620 2014.
ISSN: ISSN 0021-9258
PubMed: 24482238
DOI: 10.1074/JBC.M113.543033
Page generated: Mon Aug 12 10:24:06 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy