Atomistry » Magnesium » PDB 2mtk-2o52 » 2o2q
Atomistry »
  Magnesium »
    PDB 2mtk-2o52 »
      2o2q »

Magnesium in PDB 2o2q: Crystal Structure of the C-Terminal Domain of Rat 10'Formyltetrahydrofolate Dehydrogenase in Complex with Nadp

Enzymatic activity of Crystal Structure of the C-Terminal Domain of Rat 10'Formyltetrahydrofolate Dehydrogenase in Complex with Nadp

All present enzymatic activity of Crystal Structure of the C-Terminal Domain of Rat 10'Formyltetrahydrofolate Dehydrogenase in Complex with Nadp:
1.5.1.6;

Protein crystallography data

The structure of Crystal Structure of the C-Terminal Domain of Rat 10'Formyltetrahydrofolate Dehydrogenase in Complex with Nadp, PDB code: 2o2q was solved by Y.Tsybovsky, H.Donato, N.I.Krupenko, C.Davies, S.A.Krupenko, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.00
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 259.400, 194.500, 97.300, 90.00, 108.80, 90.00
R / Rfree (%) 16.8 / 19

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the C-Terminal Domain of Rat 10'Formyltetrahydrofolate Dehydrogenase in Complex with Nadp (pdb code 2o2q). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Crystal Structure of the C-Terminal Domain of Rat 10'Formyltetrahydrofolate Dehydrogenase in Complex with Nadp, PDB code: 2o2q:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 2o2q

Go back to Magnesium Binding Sites List in 2o2q
Magnesium binding site 1 out of 4 in the Crystal Structure of the C-Terminal Domain of Rat 10'Formyltetrahydrofolate Dehydrogenase in Complex with Nadp


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 the C-Terminal Domain of Rat 10'Formyltetrahydrofolate Dehydrogenase in Complex with Nadp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg2001

b:55.3
occ:1.00
O2N A:NAP903 2.5 36.4 0.9
O1N A:NAP903 2.9 33.8 0.9
O2A A:NAP903 3.0 24.4 0.9
PN A:NAP903 3.1 35.5 0.9
O A:HOH3149 3.4 22.2 1.0
O3 A:NAP903 3.9 28.4 0.9
NE1 A:TRP573 3.9 15.1 1.0
O A:HOH3322 3.9 44.0 1.0
PA A:NAP903 4.0 24.4 0.9
O A:HOH3266 4.0 34.0 1.0
O A:HOH3364 4.1 31.3 1.0
O A:HOH3288 4.3 32.0 1.0
O5D A:NAP903 4.6 33.2 0.9
O5B A:NAP903 4.6 23.6 0.9
CD1 A:TRP573 4.7 15.4 1.0
O1X A:NAP903 4.8 16.6 0.9
O A:HOH3255 4.8 32.4 1.0
CE2 A:TRP573 4.9 15.8 1.0

Magnesium binding site 2 out of 4 in 2o2q

Go back to Magnesium Binding Sites List in 2o2q
Magnesium binding site 2 out of 4 in the Crystal Structure of the C-Terminal Domain of Rat 10'Formyltetrahydrofolate Dehydrogenase in Complex with Nadp


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 the C-Terminal Domain of Rat 10'Formyltetrahydrofolate Dehydrogenase in Complex with Nadp within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg2002

b:64.9
occ:1.00
O2A B:NAP903 2.4 26.1 0.9
O2N B:NAP903 2.4 35.2 0.9
O1N B:NAP903 2.5 34.1 0.9
PN B:NAP903 2.7 34.5 0.9
O3 B:NAP903 3.4 28.9 0.9
PA B:NAP903 3.4 25.2 0.9
O B:HOH3204 3.9 23.8 1.0
O B:HOH3337 4.0 29.4 1.0
O B:HOH3257 4.3 31.6 1.0
O5D B:NAP903 4.3 32.9 0.9
O5B B:NAP903 4.3 25.0 0.9
NE1 B:TRP573 4.4 16.6 1.0
O B:HOH3339 4.6 30.4 1.0
O1A B:NAP903 4.6 24.9 0.9
O B:HOH3417 4.6 36.2 1.0
O B:HOH3132 5.0 29.2 1.0

Magnesium binding site 3 out of 4 in 2o2q

Go back to Magnesium Binding Sites List in 2o2q
Magnesium binding site 3 out of 4 in the Crystal Structure of the C-Terminal Domain of Rat 10'Formyltetrahydrofolate Dehydrogenase in Complex with Nadp


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 the C-Terminal Domain of Rat 10'Formyltetrahydrofolate Dehydrogenase in Complex with Nadp within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg2003

b:48.3
occ:1.00
O2N C:NAP903 2.5 35.1 0.9
O1N C:NAP903 2.7 32.9 0.9
O2A C:NAP903 2.8 22.1 0.9
PN C:NAP903 2.9 32.9 0.9
O C:HOH3407 3.4 44.1 1.0
O C:HOH3230 3.5 22.0 1.0
O3 C:NAP903 3.7 27.1 0.9
PA C:NAP903 3.8 21.1 0.9
NE1 C:TRP573 4.1 12.4 1.0
O C:HOH3376 4.1 24.0 1.0
O C:HOH3236 4.2 29.4 1.0
O5D C:NAP903 4.4 30.5 0.9
O5B C:NAP903 4.5 20.6 0.9
O C:HOH3393 4.6 38.7 1.0
NZ C:LYS757 4.9 27.8 1.0
O1X C:NAP903 4.9 18.2 0.9
CD1 C:TRP573 4.9 12.9 1.0
O1A C:NAP903 5.0 19.7 0.9

Magnesium binding site 4 out of 4 in 2o2q

Go back to Magnesium Binding Sites List in 2o2q
Magnesium binding site 4 out of 4 in the Crystal Structure of the C-Terminal Domain of Rat 10'Formyltetrahydrofolate Dehydrogenase in Complex with Nadp


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 the C-Terminal Domain of Rat 10'Formyltetrahydrofolate Dehydrogenase in Complex with Nadp within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg2004

b:54.7
occ:1.00
O2N D:NAP903 2.2 34.8 0.9
O2A D:NAP903 2.5 25.1 0.9
PN D:NAP903 2.7 34.4 0.9
O1N D:NAP903 2.7 34.8 0.9
O D:HOH3229 3.2 24.0 1.0
O3 D:NAP903 3.3 27.9 0.9
PA D:NAP903 3.4 22.9 0.9
O D:HOH3368 3.9 27.5 1.0
O D:HOH3201 4.0 31.8 1.0
NE1 D:TRP573 4.0 14.2 1.0
O5B D:NAP903 4.1 23.2 0.9
O D:HOH3470 4.3 35.3 1.0
O5D D:NAP903 4.3 32.7 0.9
O D:HOH3295 4.3 32.9 1.0
O1A D:NAP903 4.7 23.3 0.9
O1X D:NAP903 4.8 20.5 0.9
CD1 D:TRP573 4.8 15.3 1.0
O D:HOH3126 4.9 25.1 1.0

Reference:

Y.Tsybovsky, H.Donato, N.I.Krupenko, C.Davies, S.A.Krupenko. Crystal Structures of the Carboxyl Terminal Domain of Rat 10-Formyltetrahydrofolate Dehydrogenase: Implications For the Catalytic Mechanism of Aldehyde Dehydrogenases. Biochemistry V. 46 2917 2007.
ISSN: ISSN 0006-2960
PubMed: 17302434
DOI: 10.1021/BI0619573
Page generated: Mon Dec 14 07:31:34 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy