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Magnesium in PDB 4pfk: Phosphofructokinase. Structure and Control

Enzymatic activity of Phosphofructokinase. Structure and Control

All present enzymatic activity of Phosphofructokinase. Structure and Control:
2.7.1.11;

Protein crystallography data

The structure of Phosphofructokinase. Structure and Control, PDB code: 4pfk was solved by P.R.Evans, P.J.Hudson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.40
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 122.500, 84.100, 61.500, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Phosphofructokinase. Structure and Control (pdb code 4pfk). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Phosphofructokinase. Structure and Control, PDB code: 4pfk:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 4pfk

Go back to Magnesium Binding Sites List in 4pfk
Magnesium binding site 1 out of 2 in the Phosphofructokinase. Structure and Control


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Phosphofructokinase. Structure and Control within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg325

b:76.9
occ:0.50
O1A A:ADP324 2.5 49.7 0.5
O2B A:ADP324 2.5 62.1 0.5
O1B A:ADP324 2.8 59.9 0.5
O2A A:ADP324 3.0 50.9 0.5
PB A:ADP324 3.1 62.8 0.5
PA A:ADP324 3.2 51.1 0.5
O3A A:ADP324 3.6 57.0 0.5
NH2 A:ARG171 4.2 87.0 1.0
NH2 A:ARG72 4.3 98.5 1.0
NE A:ARG72 4.5 96.7 1.0
O3B A:ADP324 4.6 61.6 0.5
O5' A:ADP324 4.7 34.1 0.5
CZ A:ARG72 4.9 98.0 1.0

Magnesium binding site 2 out of 2 in 4pfk

Go back to Magnesium Binding Sites List in 4pfk
Magnesium binding site 2 out of 2 in the Phosphofructokinase. Structure and Control


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Phosphofructokinase. Structure and Control within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg327

b:35.8
occ:1.00
O2B A:ADP326 2.0 45.1 1.0
O A:GLY185 2.1 31.9 1.0
O A:HOH386 2.1 18.7 1.0
O A:HOH387 2.2 37.9 1.0
OE1 A:GLU187 2.3 38.1 1.0
O2A A:ADP326 2.4 62.7 1.0
PB A:ADP326 3.1 50.7 1.0
CD A:GLU187 3.1 37.0 1.0
C A:GLY185 3.2 26.7 1.0
OE2 A:GLU187 3.3 38.8 1.0
PA A:ADP326 3.4 57.2 1.0
O3A A:ADP326 3.4 56.1 1.0
O3B A:ADP326 3.6 52.5 1.0
CA A:GLY185 3.9 25.7 1.0
NH2 A:ARG154 3.9 44.4 1.0
N A:ALA186 4.3 28.7 1.0
O5' A:ADP326 4.3 57.5 1.0
C A:ALA186 4.3 34.2 1.0
O A:ALA186 4.4 39.8 1.0
O1B A:ADP326 4.4 46.1 1.0
O1A A:ADP326 4.4 57.9 1.0
C5' A:ADP326 4.4 53.2 1.0
NZ A:LYS213 4.5 44.0 1.0
CG A:GLU187 4.5 35.0 1.0
CA A:ALA186 4.6 32.4 1.0
NE2 A:HIS215 4.6 49.0 1.0
N A:GLU187 4.7 35.2 1.0
CZ A:ARG154 4.8 42.4 1.0

Reference:

P.R.Evans, G.W.Farrants, P.J.Hudson. Phosphofructokinase: Structure and Control. Philos.Trans.R.Soc.London, V. 293 53 1981SER.B.
ISSN: ISSN 0080-4622
PubMed: 6115424
Page generated: Tue Aug 20 01:18:21 2024

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