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Magnesium in PDB 4jjz: Crystal Strucutre of N10-Formyltetrahydrofolate Synthetase with Adp and Formylphosphate

Enzymatic activity of Crystal Strucutre of N10-Formyltetrahydrofolate Synthetase with Adp and Formylphosphate

All present enzymatic activity of Crystal Strucutre of N10-Formyltetrahydrofolate Synthetase with Adp and Formylphosphate:
6.3.4.3;

Protein crystallography data

The structure of Crystal Strucutre of N10-Formyltetrahydrofolate Synthetase with Adp and Formylphosphate, PDB code: 4jjz was solved by L.R.Celeste, L.L.Lovelace, L.Lebioda, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.81 / 2.50
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 91.170, 212.976, 53.444, 90.00, 90.00, 90.00
R / Rfree (%) 18.1 / 25.1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Strucutre of N10-Formyltetrahydrofolate Synthetase with Adp and Formylphosphate (pdb code 4jjz). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Strucutre of N10-Formyltetrahydrofolate Synthetase with Adp and Formylphosphate, PDB code: 4jjz:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 4jjz

Go back to Magnesium Binding Sites List in 4jjz
Magnesium binding site 1 out of 2 in the Crystal Strucutre of N10-Formyltetrahydrofolate Synthetase with Adp and Formylphosphate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Strucutre of N10-Formyltetrahydrofolate Synthetase with Adp and Formylphosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg605

b:29.2
occ:1.00
O4 A:XPO603 2.1 37.5 1.0
O A:HOH784 2.1 27.3 1.0
O1B A:ADP602 2.1 28.9 1.0
O A:HOH785 2.2 19.7 1.0
OG1 A:THR75 2.2 32.2 1.0
OE2 A:GLU301 2.2 34.9 1.0
PB A:ADP602 3.0 29.8 1.0
O3B A:ADP602 3.1 31.4 1.0
CD A:GLU301 3.2 37.9 1.0
P A:XPO603 3.4 42.9 1.0
CB A:THR75 3.5 30.9 1.0
OE1 A:GLU301 3.5 35.9 1.0
NH2 A:ARG97 4.0 25.4 1.0
O2B A:ADP602 4.0 31.0 1.0
N A:THR75 4.0 34.0 1.0
O1 A:XPO603 4.0 37.4 1.0
O2A A:ADP602 4.1 33.0 1.0
O3 A:XPO603 4.2 46.0 1.0
O3A A:ADP602 4.3 30.1 1.0
CA A:THR75 4.3 33.1 1.0
NZ A:LYS74 4.4 42.3 1.0
O2 A:XPO603 4.4 45.6 1.0
CG2 A:THR75 4.5 29.9 1.0
PA A:ADP602 4.5 33.4 1.0
CB A:LYS74 4.6 40.7 1.0
CG A:GLU301 4.6 38.7 1.0
O A:HOH708 4.7 21.6 1.0
CB A:ALA111 4.7 34.2 1.0
O1A A:ADP602 4.7 27.6 1.0
O A:HOH761 5.0 21.4 1.0

Magnesium binding site 2 out of 2 in 4jjz

Go back to Magnesium Binding Sites List in 4jjz
Magnesium binding site 2 out of 2 in the Crystal Strucutre of N10-Formyltetrahydrofolate Synthetase with Adp and Formylphosphate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Strucutre of N10-Formyltetrahydrofolate Synthetase with Adp and Formylphosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg606

b:24.1
occ:1.00
O1B B:ADP602 2.2 28.5 1.0
OE2 B:GLU301 2.2 32.9 1.0
O3 B:XPO603 2.2 26.3 0.5
O B:HOH774 2.2 20.4 1.0
O1 B:XPO603 2.2 21.8 0.5
O B:HOH749 2.2 20.1 1.0
OG1 B:THR75 2.2 30.9 1.0
CD B:GLU301 3.1 37.2 1.0
PB B:ADP602 3.4 31.3 1.0
OE1 B:GLU301 3.4 41.2 1.0
CB B:THR75 3.4 31.3 1.0
P B:XPO603 3.5 22.0 0.5
P B:XPO603 3.6 29.6 0.5
O3B B:ADP602 3.7 34.8 1.0
NH2 B:ARG97 3.9 27.6 1.0
N B:THR75 4.0 33.0 1.0
O3 B:XPO603 4.0 22.1 0.5
O2A B:ADP602 4.2 24.7 1.0
CA B:THR75 4.2 32.1 1.0
O1 B:XPO603 4.3 29.0 0.5
O2B B:ADP602 4.3 31.0 1.0
O4 B:XPO603 4.3 29.2 0.5
O4 B:XPO603 4.4 22.3 0.5
CG2 B:THR75 4.5 30.8 1.0
CG B:GLU301 4.5 36.1 1.0
O2 B:XPO603 4.5 24.5 0.5
O3A B:ADP602 4.5 29.1 1.0
CB B:LYS74 4.6 34.4 1.0
O2 B:XPO603 4.6 20.6 0.5
CE B:LYS74 4.7 36.2 1.0
NZ B:LYS74 4.8 37.7 1.0
O B:HOH747 4.8 16.4 1.0
PA B:ADP602 4.8 29.0 1.0
CB B:ALA111 4.8 33.1 1.0
O1A B:ADP602 5.0 26.7 1.0
C B:LYS74 5.0 32.6 1.0

Reference:

L.R.Celeste, G.Chai, M.Bielak, W.Minor, L.L.Lovelace, L.Lebioda. Mechanism of N10-Formyltetrahydrofolate Synthetase Derived From Complexes with Intermediates and Inhibitors. Protein Sci. V. 21 219 2012.
ISSN: ISSN 0961-8368
PubMed: 22109967
DOI: 10.1002/PRO.2005
Page generated: Sat Aug 17 03:11:42 2024

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