Atomistry » Magnesium » PDB 7ev3-7f68 » 7f4b
Atomistry »
  Magnesium »
    PDB 7ev3-7f68 »
      7f4b »

Magnesium in PDB 7f4b: The Crystal Structure of the Immature Apo-Enzyme of Homoserine Dehydrogenase From the Hyperthermophilic Archaeon Sulfurisphaera Tokodaii.

Enzymatic activity of The Crystal Structure of the Immature Apo-Enzyme of Homoserine Dehydrogenase From the Hyperthermophilic Archaeon Sulfurisphaera Tokodaii.

All present enzymatic activity of The Crystal Structure of the Immature Apo-Enzyme of Homoserine Dehydrogenase From the Hyperthermophilic Archaeon Sulfurisphaera Tokodaii.:
1.1.1.3;

Protein crystallography data

The structure of The Crystal Structure of the Immature Apo-Enzyme of Homoserine Dehydrogenase From the Hyperthermophilic Archaeon Sulfurisphaera Tokodaii., PDB code: 7f4b was solved by E.Kurihara, T.Kubota, K.Watanabe, K.Ogata, R.Kaneko, T.Oshima, K.Yoshimune, M.Goto, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.59 / 2.05
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 57.098, 78.305, 65.551, 90, 106.17, 90
R / Rfree (%) 23.1 / 28.1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the The Crystal Structure of the Immature Apo-Enzyme of Homoserine Dehydrogenase From the Hyperthermophilic Archaeon Sulfurisphaera Tokodaii. (pdb code 7f4b). 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 Crystal Structure of the Immature Apo-Enzyme of Homoserine Dehydrogenase From the Hyperthermophilic Archaeon Sulfurisphaera Tokodaii., PDB code: 7f4b:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 7f4b

Go back to Magnesium Binding Sites List in 7f4b
Magnesium binding site 1 out of 2 in the The Crystal Structure of the Immature Apo-Enzyme of Homoserine Dehydrogenase From the Hyperthermophilic Archaeon Sulfurisphaera Tokodaii.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The Crystal Structure of the Immature Apo-Enzyme of Homoserine Dehydrogenase From the Hyperthermophilic Archaeon Sulfurisphaera Tokodaii. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg501

b:41.7
occ:1.00
O A:LEU43 2.1 40.0 1.0
O A:HOH607 2.2 28.6 1.0
O A:HOH619 2.5 34.8 1.0
C A:LEU43 3.3 39.5 1.0
O A:GLY33 3.9 34.7 1.0
CA A:GLN44 3.9 37.4 1.0
N A:GLN44 4.0 36.3 1.0
O A:HOH668 4.3 34.3 1.0
CA A:LEU43 4.4 40.2 1.0
O A:ILE32 4.5 35.5 1.0
CB A:LEU43 4.6 39.5 1.0
C A:GLY33 4.7 35.4 1.0
CG A:GLN44 4.7 37.5 1.0
CB A:GLN44 4.8 37.1 1.0
CA A:GLY33 4.8 35.5 1.0
C A:GLN44 4.9 39.3 1.0

Magnesium binding site 2 out of 2 in 7f4b

Go back to Magnesium Binding Sites List in 7f4b
Magnesium binding site 2 out of 2 in the The Crystal Structure of the Immature Apo-Enzyme of Homoserine Dehydrogenase From the Hyperthermophilic Archaeon Sulfurisphaera Tokodaii.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of The Crystal Structure of the Immature Apo-Enzyme of Homoserine Dehydrogenase From the Hyperthermophilic Archaeon Sulfurisphaera Tokodaii. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg502

b:50.2
occ:1.00
O A:HOH662 2.0 43.6 1.0
O A:HOH613 2.1 47.0 1.0
O A:HOH608 2.1 35.4 1.0
O A:HOH602 4.2 31.4 1.0
OE2 A:GLU81 4.2 41.9 1.0
O A:ASN79 4.3 29.6 1.0
CD2 A:LEU84 4.3 31.9 1.0
O A:HOH655 4.4 45.2 1.0
CB A:ASN79 4.8 27.4 1.0

Reference:

T.Kubota, E.Kurihara, K.Watanabe, K.Ogata, R.Kaneko, M.Goto, T.Ohshima, K.Yoshimune. Conformational Changes in the Catalytic Region Are Responsible For Heat-Induced Activation of Hyperthermophilic Homoserine Dehydrogenase. Commun Biol V. 5 704 2022.
ISSN: ESSN 2399-3642
PubMed: 35835834
DOI: 10.1038/S42003-022-03656-7
Page generated: Wed Oct 2 21:10:01 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