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Magnesium in PDB 3zoz: The Structure of Human Phosphoglycerate Kinase with Bound Bromide, A Stimulating Anion.

Enzymatic activity of The Structure of Human Phosphoglycerate Kinase with Bound Bromide, A Stimulating Anion.

All present enzymatic activity of The Structure of Human Phosphoglycerate Kinase with Bound Bromide, A Stimulating Anion.:
2.7.2.3;

Protein crystallography data

The structure of The Structure of Human Phosphoglycerate Kinase with Bound Bromide, A Stimulating Anion., PDB code: 3zoz was solved by M.W.Bowler, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.95
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 38.980, 91.810, 108.210, 90.00, 90.00, 90.00
R / Rfree (%) 16.142 / 20.878

Other elements in 3zoz:

The structure of The Structure of Human Phosphoglycerate Kinase with Bound Bromide, A Stimulating Anion. also contains other interesting chemical elements:

Fluorine (F) 3 atoms
Bromine (Br) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the The Structure of Human Phosphoglycerate Kinase with Bound Bromide, A Stimulating Anion. (pdb code 3zoz). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the The Structure of Human Phosphoglycerate Kinase with Bound Bromide, A Stimulating Anion., PDB code: 3zoz:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 3zoz

Go back to Magnesium Binding Sites List in 3zoz
Magnesium binding site 1 out of 2 in the The Structure of Human Phosphoglycerate Kinase with Bound Bromide, A Stimulating Anion.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The Structure of Human Phosphoglycerate Kinase with Bound Bromide, A Stimulating Anion. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1418

b:8.0
occ:1.00
O3B A:ADP1422 2.0 7.6 1.0
F1 A:MGF1420 2.0 9.2 1.0
O A:HOH2241 2.0 5.9 1.0
OD2 A:ASP375 2.1 8.2 1.0
O2A A:ADP1422 2.1 7.2 1.0
O A:HOH2400 2.1 8.4 1.0
PB A:ADP1422 3.1 7.2 1.0
CG A:ASP375 3.2 9.1 1.0
PA A:ADP1422 3.2 7.3 1.0
MG A:MGF1420 3.5 11.0 1.0
O3A A:ADP1422 3.5 7.8 1.0
O2B A:ADP1422 3.7 7.3 1.0
O A:HOH2427 3.8 9.0 1.0
CB A:ASP375 3.8 8.8 1.0
NZ A:LYS216 3.9 7.5 1.0
N A:ASP375 4.0 8.5 1.0
O A:HOH2398 4.1 16.1 1.0
CE A:LYS216 4.1 8.0 1.0
O2 A:3PG1421 4.1 8.1 1.0
OD1 A:ASP375 4.2 8.6 1.0
O A:HOH2023 4.2 25.4 1.0
C5' A:ADP1422 4.2 8.0 1.0
O5' A:ADP1422 4.3 7.8 1.0
O A:HOH2047 4.4 12.3 1.0
O1A A:ADP1422 4.4 8.1 1.0
O1B A:ADP1422 4.5 7.3 1.0
O A:HOH2399 4.5 19.5 1.0
F2 A:MGF1420 4.5 10.4 1.0
CA A:ASP375 4.6 8.9 1.0
CD A:LYS216 4.7 8.1 1.0
O1 A:3PG1421 4.7 7.8 1.0
N A:GLY374 4.8 8.2 1.0
C1 A:3PG1421 4.8 7.9 1.0
C A:GLY374 4.9 8.4 1.0
CA A:GLY374 4.9 8.2 1.0

Magnesium binding site 2 out of 2 in 3zoz

Go back to Magnesium Binding Sites List in 3zoz
Magnesium binding site 2 out of 2 in the The Structure of Human Phosphoglycerate Kinase with Bound Bromide, A Stimulating Anion.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of The Structure of Human Phosphoglycerate Kinase with Bound Bromide, A Stimulating Anion. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1420

b:11.0
occ:1.00
MG A:MGF1420 0.0 11.0 1.0
F1 A:MGF1420 1.9 9.2 1.0
F2 A:MGF1420 2.0 10.4 1.0
F3 A:MGF1420 2.0 11.0 1.0
O2B A:ADP1422 2.1 7.3 1.0
O1 A:3PG1421 2.2 7.8 1.0
C1 A:3PG1421 3.0 7.9 1.0
PB A:ADP1422 3.1 7.2 1.0
O3B A:ADP1422 3.2 7.6 1.0
O2 A:3PG1421 3.2 8.1 1.0
MG A:MG1418 3.5 8.0 1.0
O A:HOH2400 3.7 8.4 1.0
O A:HOH2194 3.9 9.6 1.0
NZ A:LYS220 3.9 8.5 1.0
NZ A:LYS216 3.9 7.5 1.0
O A:HOH2197 4.0 6.8 1.0
CA A:GLY396 4.1 7.9 1.0
N A:GLY374 4.1 8.2 1.0
O2A A:ADP1422 4.2 7.2 1.0
O3A A:ADP1422 4.2 7.8 1.0
O1B A:ADP1422 4.2 7.3 1.0
NH2 A:ARG39 4.2 8.4 1.0
N A:GLY397 4.2 8.3 1.0
C2 A:3PG1421 4.4 8.2 1.0
N A:GLY396 4.5 8.2 1.0
CA A:GLY373 4.5 8.2 1.0
PA A:ADP1422 4.5 7.3 1.0
OD1 A:ASN337 4.7 8.4 1.0
CD A:LYS216 4.7 8.1 1.0
C A:GLY396 4.7 8.1 1.0
CE A:LYS216 4.7 8.0 1.0
O1A A:ADP1422 4.7 8.1 1.0
O A:HOH2241 4.8 5.9 1.0
CE A:LYS220 4.8 8.5 1.0
C A:GLY373 4.8 8.3 1.0

Reference:

M.W.Bowler, M.W.Bowler. N/A N/A.
Page generated: Thu Aug 15 14:01:31 2024

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