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Magnesium in PDB 6vmv: Crystal Structure of the H767A Mutant of Goxa Soaked with Glycine

Protein crystallography data

The structure of Crystal Structure of the H767A Mutant of Goxa Soaked with Glycine, PDB code: 6vmv was solved by E.T.Yukl, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.20 / 2.20
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 109.965, 93.081, 187.642, 90.00, 95.07, 90.00
R / Rfree (%) 18.7 / 23.9

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the H767A Mutant of Goxa Soaked with Glycine (pdb code 6vmv). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Crystal Structure of the H767A Mutant of Goxa Soaked with Glycine, PDB code: 6vmv:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 6vmv

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Magnesium binding site 1 out of 4 in the Crystal Structure of the H767A Mutant of Goxa Soaked with Glycine


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of the H767A Mutant of Goxa Soaked with Glycine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg901

b:37.0
occ:1.00
O A:ALA362 2.2 33.5 1.0
O A:HOH1063 2.2 36.4 1.0
O A:ILE365 2.3 31.6 1.0
O A:ALA699 2.4 31.4 1.0
OD1 A:ASN700 2.6 34.9 1.0
OD1 A:ASP360 2.7 25.9 1.0
C A:ALA362 3.2 29.2 1.0
C A:ALA699 3.4 30.6 1.0
C A:ILE365 3.5 31.9 1.0
CG A:ASP360 3.5 36.4 1.0
OD2 A:ASP360 3.6 34.9 1.0
CG A:ASN700 3.6 28.4 1.0
CA A:ASN700 3.9 23.1 1.0
N A:ASN700 4.0 24.1 1.0
N A:PRO363 4.0 22.6 1.0
CA A:PRO363 4.0 30.3 1.0
CA A:ALA362 4.0 35.5 1.0
N A:ILE365 4.1 29.5 1.0
CB A:ALA362 4.1 32.0 1.0
C A:PRO363 4.2 39.1 1.0
CA A:ILE365 4.2 29.9 1.0
N A:ALA362 4.3 37.9 1.0
CB A:ILE365 4.3 33.3 1.0
CB A:ASN700 4.3 31.5 1.0
O A:PRO363 4.3 45.9 1.0
CB A:ALA699 4.4 28.3 1.0
CA A:ALA699 4.4 26.8 1.0
N A:GLU366 4.5 31.3 1.0
ND2 A:ASN700 4.6 35.1 1.0
CD A:PRO367 4.8 30.4 1.0
CA A:GLU366 4.8 27.7 1.0
N A:GLN364 4.8 43.8 1.0
CB A:ASP360 5.0 31.7 1.0

Magnesium binding site 2 out of 4 in 6vmv

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Magnesium binding site 2 out of 4 in the Crystal Structure of the H767A Mutant of Goxa Soaked with Glycine


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of the H767A Mutant of Goxa Soaked with Glycine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg901

b:52.0
occ:1.00
O B:ILE365 2.2 39.1 1.0
O B:ALA362 2.3 49.1 1.0
O B:HOH1035 2.4 44.4 1.0
O B:ALA699 2.5 40.1 1.0
OD1 B:ASN700 2.6 52.3 1.0
OD1 B:ASP360 3.0 47.0 1.0
C B:ALA362 3.2 39.6 1.0
C B:ILE365 3.3 39.2 1.0
C B:ALA699 3.4 43.8 1.0
OD2 B:ASP360 3.6 60.9 1.0
CG B:ASP360 3.7 52.2 1.0
CG B:ASN700 3.7 50.0 1.0
N B:ILE365 3.9 39.4 1.0
CA B:ILE365 4.0 36.8 1.0
CB B:ALA362 4.0 31.7 1.0
CA B:ASN700 4.0 45.3 1.0
CA B:ALA362 4.1 43.3 1.0
CB B:ILE365 4.1 40.0 1.0
N B:PRO363 4.1 43.6 1.0
CA B:PRO363 4.1 44.8 1.0
N B:ASN700 4.1 37.5 1.0
C B:PRO363 4.2 46.4 1.0
N B:ALA362 4.3 42.7 1.0
CB B:ALA699 4.3 40.0 1.0
O B:PRO363 4.3 45.9 1.0
CA B:ALA699 4.4 43.6 1.0
N B:GLU366 4.4 41.1 1.0
CB B:ASN700 4.5 42.8 1.0
ND2 B:ASN700 4.6 46.7 1.0
CA B:GLU366 4.7 40.2 1.0
CG2 B:ILE365 4.7 40.4 1.0
CD B:PRO367 4.8 35.0 1.0
N B:GLN364 4.8 40.9 1.0
C B:GLN364 5.0 43.7 1.0

Magnesium binding site 3 out of 4 in 6vmv

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Magnesium binding site 3 out of 4 in the Crystal Structure of the H767A Mutant of Goxa Soaked with Glycine


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of the H767A Mutant of Goxa Soaked with Glycine within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg901

b:41.4
occ:1.00
O C:ALA699 2.3 32.8 1.0
O C:ALA362 2.3 35.5 1.0
O C:ILE365 2.3 32.1 1.0
O C:HOH1014 2.4 40.9 1.0
OD1 C:ASN700 2.6 35.2 1.0
OD1 C:ASP360 2.7 31.6 1.0
C C:ALA362 3.2 31.1 1.0
C C:ALA699 3.3 29.7 1.0
OD2 C:ASP360 3.3 39.6 1.0
CG C:ASP360 3.4 40.4 1.0
C C:ILE365 3.5 31.6 1.0
CG C:ASN700 3.7 30.1 1.0
CA C:ASN700 3.8 23.5 1.0
N C:ASN700 3.9 28.9 1.0
CB C:ALA362 3.9 25.4 1.0
CA C:ALA362 3.9 27.1 1.0
N C:PRO363 4.0 24.9 1.0
N C:ILE365 4.1 41.7 1.0
CA C:PRO363 4.1 27.1 1.0
N C:ALA362 4.1 33.8 1.0
CA C:ILE365 4.2 34.0 1.0
C C:PRO363 4.3 35.1 1.0
CB C:ILE365 4.3 27.6 1.0
CA C:ALA699 4.3 28.9 1.0
CB C:ASN700 4.3 29.9 1.0
CB C:ALA699 4.4 31.3 1.0
N C:GLU366 4.5 29.8 1.0
O C:PRO363 4.5 40.2 1.0
ND2 C:ASN700 4.7 35.5 1.0
N C:GLN364 4.8 36.7 1.0
CA C:GLU366 4.8 31.4 1.0
CB C:ASP360 4.9 36.7 1.0
CD C:PRO367 4.9 24.2 1.0
C C:ASN700 5.0 27.7 1.0

Magnesium binding site 4 out of 4 in 6vmv

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Magnesium binding site 4 out of 4 in the Crystal Structure of the H767A Mutant of Goxa Soaked with Glycine


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Crystal Structure of the H767A Mutant of Goxa Soaked with Glycine within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg901

b:43.8
occ:1.00
O D:ILE365 2.4 35.7 1.0
O D:ALA699 2.4 39.1 1.0
O D:ALA362 2.4 46.2 1.0
OD1 D:ASN700 2.4 46.6 1.0
O D:HOH1081 2.6 34.2 1.0
OD1 D:ASP360 2.8 42.2 1.0
C D:ALA699 3.3 33.5 1.0
C D:ALA362 3.3 43.0 1.0
OD2 D:ASP360 3.4 44.6 1.0
CG D:ASP360 3.5 38.2 1.0
C D:ILE365 3.5 38.7 1.0
CG D:ASN700 3.6 40.6 1.0
CA D:ASN700 3.8 38.5 1.0
N D:ASN700 3.9 33.1 1.0
CA D:PRO363 4.1 43.6 1.0
N D:ILE365 4.1 41.5 1.0
N D:PRO363 4.1 40.9 1.0
CA D:ALA362 4.2 44.0 1.0
CA D:ILE365 4.2 42.1 1.0
CB D:ALA362 4.2 39.8 1.0
CB D:ILE365 4.2 39.9 1.0
CB D:ALA699 4.3 41.0 1.0
CB D:ASN700 4.3 34.3 1.0
N D:ALA362 4.3 35.1 1.0
CA D:ALA699 4.3 34.6 1.0
C D:PRO363 4.4 47.4 1.0
N D:GLU366 4.6 40.6 1.0
ND2 D:ASN700 4.6 47.1 1.0
O D:PRO363 4.6 45.0 1.0
CA D:GLU366 4.8 39.2 1.0
CD D:PRO367 4.8 41.1 1.0
N D:GLN364 4.9 38.6 1.0
CG2 D:ILE365 4.9 41.9 1.0
CB D:ASP360 4.9 32.9 1.0
O D:ALA576 5.0 49.6 1.0

Reference:

K.J.Mamounis, E.T.Yukl, V.L.Davidson. Roles of Active Site Residues in Catalysis, Substrate Binding, Cooperativity and the Reaction Mechanism of the Quinoprotein Glycine Oxidase J.Biol.Chem. 2020.
ISSN: ESSN 1083-351X
Page generated: Tue Oct 1 22:08:03 2024

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