Atomistry » Magnesium » PDB 4cgl-4cs4 » 4co9
Atomistry »
  Magnesium »
    PDB 4cgl-4cs4 »
      4co9 »

Magnesium in PDB 4co9: Crystal Structure of Kynurenine Formamidase From Bacillus Anthracis

Enzymatic activity of Crystal Structure of Kynurenine Formamidase From Bacillus Anthracis

All present enzymatic activity of Crystal Structure of Kynurenine Formamidase From Bacillus Anthracis:
3.5.1.9;

Protein crystallography data

The structure of Crystal Structure of Kynurenine Formamidase From Bacillus Anthracis, PDB code: 4co9 was solved by L.Diaz-Saez, V.Srikannathasan, M.Zoltner, W.N.Hunter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 83.76 / 1.95
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 73.710, 66.020, 83.760, 90.00, 90.32, 90.00
R / Rfree (%) 17.145 / 20.663

Other elements in 4co9:

The structure of Crystal Structure of Kynurenine Formamidase From Bacillus Anthracis also contains other interesting chemical elements:

Zinc (Zn) 8 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Kynurenine Formamidase From Bacillus Anthracis (pdb code 4co9). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 5 binding sites of Magnesium where determined in the Crystal Structure of Kynurenine Formamidase From Bacillus Anthracis, PDB code: 4co9:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5;

Magnesium binding site 1 out of 5 in 4co9

Go back to Magnesium Binding Sites List in 4co9
Magnesium binding site 1 out of 5 in the Crystal Structure of Kynurenine Formamidase From Bacillus Anthracis


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Kynurenine Formamidase From Bacillus Anthracis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1210

b:40.7
occ:1.00
 O A:HOH2088 1.9 23.3 1.0
O A:HOH2288 2.0 35.1 1.0
O A:GLY38 2.0 18.9 1.0
O A:HOH2091 2.1 34.0 1.0
O A:HOH2089 2.5 30.4 1.0
O A:HOH2090 2.7 34.3 1.0
C A:GLY38 3.2 18.1 1.0
O A:HOH2287 3.5 56.8 1.0
CA A:GLY38 4.0 18.1 1.0
N A:SER39 4.1 17.3 1.0
CA A:SER39 4.2 17.4 1.0
O A:HOH2079 4.4 21.3 1.0
O B:LYS156 4.5 37.3 1.0
CB A:SER39 4.6 18.6 1.0
OE2 B:GLU157 4.6 47.1 1.0
OE1 B:GLU157 4.9 46.3 1.0

Magnesium binding site 2 out of 5 in 4co9

Go back to Magnesium Binding Sites List in 4co9
Magnesium binding site 2 out of 5 in the Crystal Structure of Kynurenine Formamidase From Bacillus Anthracis


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Kynurenine Formamidase From Bacillus Anthracis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1214

b:21.1
occ:1.00
 O A:HOH2124 2.0 22.3 1.0
O A:HOH2292 2.1 20.6 1.0
O A:HOH2291 2.1 23.9 1.0
O A:HOH2123 2.2 14.7 1.0
O A:HOH2119 2.2 28.6 1.0
O A:HOH2293 2.2 15.9 1.0
OD1 A:ASP64 3.9 19.4 1.0
O A:ASN63 4.8 18.4 1.0

Magnesium binding site 3 out of 5 in 4co9

Go back to Magnesium Binding Sites List in 4co9
Magnesium binding site 3 out of 5 in the Crystal Structure of Kynurenine Formamidase From Bacillus Anthracis


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of Kynurenine Formamidase From Bacillus Anthracis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1215

b:28.6
occ:1.00
 O D:HOH2087 1.9 23.2 1.0
O A:HOH2296 2.1 38.9 1.0
O A:HOH2269 2.1 12.0 1.0
O D:HOH2085 2.1 35.2 1.0
O A:HOH2294 2.3 23.4 1.0
O A:HOH2295 2.5 21.7 1.0
O A:HOH2289 3.9 26.4 1.0
O D:HOH2086 3.9 35.5 1.0
OD2 A:ASP182 4.1 11.2 1.0
O A:HOH2157 4.1 17.3 1.0
OD1 D:ASP64 4.1 13.3 1.0
CB A:ASP182 4.2 10.6 1.0
O A:HOH2158 4.3 9.5 1.0
O D:HOH2084 4.4 6.2 1.0
CG A:ASP182 4.7 10.6 1.0
O D:HOH2091 4.7 22.2 1.0
CA D:ASP64 4.8 10.3 1.0

Magnesium binding site 4 out of 5 in 4co9

Go back to Magnesium Binding Sites List in 4co9
Magnesium binding site 4 out of 5 in the Crystal Structure of Kynurenine Formamidase From Bacillus Anthracis


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Crystal Structure of Kynurenine Formamidase From Bacillus Anthracis within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg1210

b:27.9
occ:1.00
 O C:HOH2087 2.0 20.4 1.0
O C:GLY38 2.0 14.3 1.0
O C:HOH2088 2.1 16.9 1.0
O C:HOH2237 2.2 21.1 1.0
O C:HOH2089 2.2 22.9 1.0
O C:HOH2086 2.4 19.6 1.0
C C:GLY38 3.1 13.6 1.0
CA C:GLY38 3.9 13.1 1.0
O C:HOH2077 4.0 15.4 1.0
N C:SER39 4.1 13.2 1.0
CA C:SER39 4.2 13.2 1.0
O D:LYS156 4.4 24.8 1.0
O C:HOH2029 4.4 24.4 1.0
OE2 D:GLU157 4.4 27.4 1.0
OE1 D:GLU157 4.6 29.8 1.0
CB C:SER39 4.6 14.5 1.0
O D:HOH2169 4.8 29.1 1.0
CD D:GLU157 4.9 27.2 1.0

Magnesium binding site 5 out of 5 in 4co9

Go back to Magnesium Binding Sites List in 4co9
Magnesium binding site 5 out of 5 in the Crystal Structure of Kynurenine Formamidase From Bacillus Anthracis


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of Crystal Structure of Kynurenine Formamidase From Bacillus Anthracis within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg1211

b:47.1
occ:1.00
 O C:HOH2238 1.9 39.0 1.0
O C:HOH2109 2.1 28.2 1.0
O C:HOH2239 2.2 28.3 1.0
O C:HOH2240 2.3 39.0 1.0
O C:HOH2108 2.4 28.0 1.0
O C:HOH2118 2.6 48.0 1.0
OD2 C:ASP64 4.0 22.3 1.0
OD2 C:ASP62 4.2 18.4 1.0
OD1 C:ASP62 4.3 15.6 1.0
CB C:ASP64 4.6 18.0 1.0
CG C:ASP62 4.7 16.3 1.0
CG C:ASP64 4.8 19.7 1.0
O C:HOH2119 4.9 36.1 1.0

Reference:

L.Diaz-Saez, V.Srikannathasan, M.Zoltner, W.N.Hunter. Structure of Bacterial Kynurenine Formamidase Reveals A Crowded Binuclear-Zinc Catalytic Site Primed to Generate A Potent Nucleophile. Biochem.J. V. 462 581 2014.
ISSN: ISSN 0264-6021
PubMed: 24942958
DOI: 10.1042/BJ20140511
Page generated: Thu Aug 15 16:49:53 2024

Last articles

Zn in 9MJ5
Zn in 9HNW
Zn in 9G0L
Zn in 9FNE
Zn in 9DZN
Zn in 9E0I
Zn in 9D32
Zn in 9DAK
Zn in 8ZXC
Zn in 8ZUF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy