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Magnesium in PDB 1xd9: Crystal Structure of the Nitrogenase Fe Protein ASP39ASN with Mgadp Bound

Enzymatic activity of Crystal Structure of the Nitrogenase Fe Protein ASP39ASN with Mgadp Bound

All present enzymatic activity of Crystal Structure of the Nitrogenase Fe Protein ASP39ASN with Mgadp Bound:
1.18.6.1;

Protein crystallography data

The structure of Crystal Structure of the Nitrogenase Fe Protein ASP39ASN with Mgadp Bound, PDB code: 1xd9 was solved by S.B.Jang, M.S.Jeong, L.C.Seefeldt, J.W.Peters, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.80
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 57.052, 92.214, 61.375, 90.00, 101.23, 90.00
R / Rfree (%) 22.9 / 29.9

Other elements in 1xd9:

The structure of Crystal Structure of the Nitrogenase Fe Protein ASP39ASN with Mgadp Bound also contains other interesting chemical elements:

Iron (Fe) 4 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Nitrogenase Fe Protein ASP39ASN with Mgadp Bound (pdb code 1xd9). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of the Nitrogenase Fe Protein ASP39ASN with Mgadp Bound, PDB code: 1xd9:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1xd9

Go back to Magnesium Binding Sites List in 1xd9
Magnesium binding site 1 out of 2 in the Crystal Structure of the Nitrogenase Fe Protein ASP39ASN with Mgadp Bound


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 Nitrogenase Fe Protein ASP39ASN with Mgadp Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg293

b:49.8
occ:1.00
OG A:SER16 2.5 50.3 1.0
OD2 A:ASP43 2.5 68.6 1.0
CG A:ASP43 2.9 72.9 1.0
OD1 A:ASP43 3.0 74.6 1.0
O1B A:ADP291 3.4 75.4 1.0
NZ A:LYS15 3.6 50.5 1.0
OG A:SER44 3.7 70.2 1.0
CB A:SER16 3.7 53.0 1.0
ND2 A:ASN39 3.9 64.3 1.0
O2B A:ADP291 4.0 79.7 1.0
CB A:ASP43 4.1 66.0 1.0
C A:ASP43 4.2 62.7 1.0
PB A:ADP291 4.3 75.8 1.0
OD2 A:ASP125 4.3 56.2 1.0
N A:SER44 4.4 64.2 1.0
O A:ASP43 4.4 59.2 1.0
CB A:SER44 4.5 70.0 1.0
CA A:SER44 4.5 67.4 1.0
CB A:ASN39 4.5 66.6 1.0
CG A:ASN39 4.5 64.7 1.0
CA A:ASP43 4.7 61.7 1.0
O1A A:ADP291 4.8 77.5 1.0
CA A:SER16 4.9 54.1 1.0
CE A:LYS15 4.9 52.1 1.0

Magnesium binding site 2 out of 2 in 1xd9

Go back to Magnesium Binding Sites List in 1xd9
Magnesium binding site 2 out of 2 in the Crystal Structure of the Nitrogenase Fe Protein ASP39ASN with Mgadp Bound


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 Nitrogenase Fe Protein ASP39ASN with Mgadp Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg294

b:57.6
occ:1.00
OD2 B:ASP43 2.5 64.8 1.0
OG B:SER16 2.5 69.5 1.0
OD1 B:ASP43 2.7 71.4 1.0
CG B:ASP43 2.7 68.5 1.0
O2B B:ADP292 3.1 79.6 1.0
CB B:SER16 3.6 71.6 1.0
O3B B:ADP292 3.8 85.5 1.0
NZ B:LYS15 3.9 48.2 1.0
CB B:ASP43 3.9 66.8 1.0
OG B:SER44 3.9 77.4 1.0
PB B:ADP292 3.9 87.3 1.0
C B:ASP43 4.0 69.9 1.0
O B:ASP43 4.1 68.8 1.0
ND2 B:ASN39 4.3 69.3 1.0
N B:SER44 4.3 72.3 1.0
CA B:ASP43 4.5 67.7 1.0
CA B:SER44 4.5 77.3 1.0
O2A B:ADP292 4.5 90.3 1.0
OD2 B:ASP125 4.6 59.1 1.0
CB B:SER44 4.6 75.7 1.0
CA B:SER16 4.8 68.9 1.0
CB B:ASN39 4.9 67.0 1.0
CG B:ASN39 4.9 69.0 1.0
N B:ASP43 4.9 70.2 1.0
N B:SER16 5.0 69.0 1.0
O3A B:ADP292 5.0 84.9 1.0

Reference:

S.B.Jang, M.S.Jeong, L.C.Seefeldt, J.W.Peters. Structural and Biochemical Implications of Single Amino Acid Substitutions in the Nucleotide-Dependent Switch Regions of the Nitrogenase Fe Protein From Azotobacter Vinelandii J.Biol.Inorg.Chem. V. 9 1028 2004.
ISSN: ISSN 0949-8257
PubMed: 15549494
DOI: 10.1007/S00775-004-0605-5
Page generated: Tue Aug 13 17:31:01 2024

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