Atomistry » Magnesium » PDB 3brw-3c5h » 3c1m
Atomistry »
  Magnesium »
    PDB 3brw-3c5h »
      3c1m »

Magnesium in PDB 3c1m: Cyrstal Structure of Threonine-Sensitive Aspartokinase From Methanococcus Jannaschii with Mgamp-Pnp and L-Aspartate

Enzymatic activity of Cyrstal Structure of Threonine-Sensitive Aspartokinase From Methanococcus Jannaschii with Mgamp-Pnp and L-Aspartate

All present enzymatic activity of Cyrstal Structure of Threonine-Sensitive Aspartokinase From Methanococcus Jannaschii with Mgamp-Pnp and L-Aspartate:
2.7.2.4;

Protein crystallography data

The structure of Cyrstal Structure of Threonine-Sensitive Aspartokinase From Methanococcus Jannaschii with Mgamp-Pnp and L-Aspartate, PDB code: 3c1m was solved by X.Liu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.30
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 101.408, 104.478, 192.045, 90.00, 90.00, 90.00
R / Rfree (%) 19.4 / 24.6

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Cyrstal Structure of Threonine-Sensitive Aspartokinase From Methanococcus Jannaschii with Mgamp-Pnp and L-Aspartate (pdb code 3c1m). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Cyrstal Structure of Threonine-Sensitive Aspartokinase From Methanococcus Jannaschii with Mgamp-Pnp and L-Aspartate, PDB code: 3c1m:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 3c1m

Go back to Magnesium Binding Sites List in 3c1m
Magnesium binding site 1 out of 4 in the Cyrstal Structure of Threonine-Sensitive Aspartokinase From Methanococcus Jannaschii with Mgamp-Pnp and L-Aspartate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Cyrstal Structure of Threonine-Sensitive Aspartokinase From Methanococcus Jannaschii with Mgamp-Pnp and L-Aspartate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1

b:32.3
occ:1.00
 O1A A:ANP472 2.0 29.5 1.0
O1G A:ANP472 2.0 32.7 1.0
O A:HOH533 2.0 23.6 1.0
O2B A:ANP472 2.1 27.7 1.0
O A:HOH512 2.1 24.0 1.0
O A:HOH514 2.2 21.9 1.0
PB A:ANP472 3.2 26.3 1.0
PG A:ANP472 3.2 30.5 1.0
PA A:ANP472 3.2 28.0 1.0
N3B A:ANP472 3.5 28.8 1.0
O3A A:ANP472 3.6 28.1 1.0
O2G A:ANP472 3.6 30.8 1.0
O5' A:ANP472 3.9 28.3 1.0
O A:HOH501 4.0 34.0 1.0
O A:HOH638 4.0 43.2 1.0
OD2 A:ASP211 4.1 22.2 1.0
O A:LYS266 4.2 22.0 1.0
OD1 A:ASP471 4.3 37.8 1.0
OD2 A:ASP471 4.3 35.7 1.0
NZ A:LYS6 4.3 19.8 1.0
O A:HOH556 4.3 36.0 1.0
O3G A:ANP472 4.4 31.6 1.0
CA A:GLY208 4.5 21.6 1.0
O2A A:ANP472 4.5 30.5 1.0
O1B A:ANP472 4.6 24.7 1.0
OD1 A:ASP211 4.6 21.9 1.0
CG A:ASP211 4.7 21.8 1.0
CG A:ASP471 4.7 35.8 1.0
O A:GLY208 4.8 21.4 1.0
O A:VAL267 5.0 22.6 1.0

Magnesium binding site 2 out of 4 in 3c1m

Go back to Magnesium Binding Sites List in 3c1m
Magnesium binding site 2 out of 4 in the Cyrstal Structure of Threonine-Sensitive Aspartokinase From Methanococcus Jannaschii with Mgamp-Pnp and L-Aspartate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Cyrstal Structure of Threonine-Sensitive Aspartokinase From Methanococcus Jannaschii with Mgamp-Pnp and L-Aspartate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg471

b:30.0
occ:1.00
 O1G B:ANP473 2.0 35.5 1.0
O B:HOH509 2.1 29.9 1.0
O B:HOH545 2.1 24.9 1.0
O3A B:ANP473 2.1 43.7 1.0
O B:HOH504 2.2 29.5 1.0
O2B B:ANP473 2.6 42.4 1.0
PB B:ANP473 3.0 39.4 1.0
PG B:ANP473 3.2 36.3 1.0
PA B:ANP473 3.5 39.9 1.0
N3B B:ANP473 3.6 38.8 1.0
O2G B:ANP473 3.8 33.8 1.0
O1A B:ANP473 3.9 43.1 1.0
O5' B:ANP473 3.9 40.8 1.0
O B:HOH590 4.0 31.9 1.0
O B:LYS266 4.1 21.2 1.0
O B:HOH517 4.1 40.2 1.0
OD2 B:ASP211 4.2 19.3 1.0
OD2 B:ASP472 4.3 34.4 1.0
O B:HOH614 4.3 33.0 1.0
O B:HOH620 4.3 48.1 1.0
OD1 B:ASP472 4.3 34.2 1.0
O1B B:ANP473 4.3 42.6 1.0
NZ B:LYS6 4.4 13.5 1.0
O3G B:ANP473 4.5 34.9 1.0
O2A B:ANP473 4.5 46.5 1.0
CA B:GLY208 4.6 19.4 1.0
OD1 B:ASP211 4.7 21.3 1.0
CG B:ASP472 4.7 35.1 1.0
CG B:LYS266 4.8 22.9 1.0
CG B:ASP211 4.8 20.2 1.0
O B:GLY208 4.8 19.4 1.0
CE B:LYS266 4.9 24.3 1.0
O B:HOH594 4.9 37.7 1.0

Magnesium binding site 3 out of 4 in 3c1m

Go back to Magnesium Binding Sites List in 3c1m
Magnesium binding site 3 out of 4 in the Cyrstal Structure of Threonine-Sensitive Aspartokinase From Methanococcus Jannaschii with Mgamp-Pnp and L-Aspartate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Cyrstal Structure of Threonine-Sensitive Aspartokinase From Methanococcus Jannaschii with Mgamp-Pnp and L-Aspartate within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg471

b:45.0
occ:1.00
 O C:HOH547 2.1 42.6 1.0
O C:HOH520 2.1 34.5 1.0
O1A C:ANP473 2.2 48.0 1.0
O1G C:ANP473 2.3 43.5 1.0
O2B C:ANP473 2.8 46.1 1.0
O3A C:ANP473 3.2 47.5 1.0
PA C:ANP473 3.3 46.1 1.0
PB C:ANP473 3.4 45.5 1.0
PG C:ANP473 3.4 42.1 1.0
N3B C:ANP473 3.7 43.5 1.0
O2G C:ANP473 3.8 41.2 1.0
O C:HOH587 3.9 39.4 1.0
O C:LYS266 3.9 22.4 1.0
O C:HOH591 4.0 36.3 1.0
OD2 C:ASP211 4.0 21.6 1.0
OXT C:ASP472 4.1 39.6 1.0
O5' C:ANP473 4.1 47.2 1.0
O C:ASP472 4.3 39.4 1.0
CA C:GLY208 4.4 23.3 1.0
NZ C:LYS6 4.4 17.6 1.0
O2A C:ANP473 4.6 49.3 1.0
C C:ASP472 4.7 39.5 1.0
CG C:ASP211 4.7 22.1 1.0
O3G C:ANP473 4.7 43.2 1.0
OD1 C:ASP211 4.7 22.6 1.0
O C:GLY208 4.8 23.8 1.0
O1B C:ANP473 4.9 46.3 1.0
CE C:LYS266 4.9 23.3 1.0
CG C:LYS266 4.9 23.0 1.0

Magnesium binding site 4 out of 4 in 3c1m

Go back to Magnesium Binding Sites List in 3c1m
Magnesium binding site 4 out of 4 in the Cyrstal Structure of Threonine-Sensitive Aspartokinase From Methanococcus Jannaschii with Mgamp-Pnp and L-Aspartate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Cyrstal Structure of Threonine-Sensitive Aspartokinase From Methanococcus Jannaschii with Mgamp-Pnp and L-Aspartate within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg471

b:22.8
occ:1.00
 O1A D:ANP473 2.0 29.1 1.0
O D:HOH537 2.0 18.5 1.0
O D:HOH522 2.1 24.7 1.0
O1G D:ANP473 2.1 30.4 1.0
O D:HOH498 2.1 24.7 1.0
O2B D:ANP473 2.2 27.4 1.0
PG D:ANP473 3.3 29.8 1.0
PB D:ANP473 3.3 28.2 1.0
PA D:ANP473 3.3 28.1 1.0
N3B D:ANP473 3.7 29.1 1.0
O3A D:ANP473 3.7 27.8 1.0
O2G D:ANP473 3.7 30.2 1.0
OD2 D:ASP211 3.9 20.1 1.0
O D:HOH507 4.0 30.4 1.0
O D:HOH541 4.1 35.9 1.0
O5' D:ANP473 4.1 28.6 1.0
OD2 D:ASP472 4.1 30.8 1.0
O D:LYS266 4.2 21.6 1.0
O D:HOH506 4.2 29.0 1.0
OD1 D:ASP472 4.2 33.4 1.0
CA D:GLY208 4.4 19.9 1.0
NZ D:LYS6 4.4 15.6 1.0
O2A D:ANP473 4.5 30.2 1.0
O3G D:ANP473 4.5 27.3 1.0
CG D:ASP472 4.6 30.9 1.0
O D:GLY208 4.6 20.1 1.0
O1B D:ANP473 4.6 28.1 1.0
CG D:ASP211 4.7 20.1 1.0
CE D:LYS266 4.8 25.8 1.0
OD1 D:ASP211 4.8 19.3 1.0
C D:GLY208 4.9 19.7 1.0
O D:HOH553 5.0 39.3 1.0

Reference:

X.Liu, A.G.Pavlovsky, R.E.Viola. The Structural Basis For Allosteric Inhibition of A Threonine-Sensitive Aspartokinase. J.Biol.Chem. V. 283 16216 2008.
ISSN: ISSN 0021-9258
PubMed: 18334478
DOI: 10.1074/JBC.M800760200
Page generated: Wed Aug 14 09:24:47 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy