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Magnesium in PDB 2c8v: Insights Into the Role of Nucleotide-Dependent Conformational Change in Nitrogenase Catalysis: Structural Characterization of the Nitrogenase Fe Protein LEU127 Deletion Variant with Bound Mgatp

Enzymatic activity of Insights Into the Role of Nucleotide-Dependent Conformational Change in Nitrogenase Catalysis: Structural Characterization of the Nitrogenase Fe Protein LEU127 Deletion Variant with Bound Mgatp

All present enzymatic activity of Insights Into the Role of Nucleotide-Dependent Conformational Change in Nitrogenase Catalysis: Structural Characterization of the Nitrogenase Fe Protein LEU127 Deletion Variant with Bound Mgatp:
1.18.6.1;

Protein crystallography data

The structure of Insights Into the Role of Nucleotide-Dependent Conformational Change in Nitrogenase Catalysis: Structural Characterization of the Nitrogenase Fe Protein LEU127 Deletion Variant with Bound Mgatp, PDB code: 2c8v was solved by S.Sen, A.Krishnakumar, J.Mcclead, M.K.Johnson, L.C.Seefeldt, R.K.Szilagyi, J.W.Peters, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 2.50
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 70.900, 133.300, 61.500, 90.00, 90.00, 90.00
R / Rfree (%) 23.81 / 27.93

Other elements in 2c8v:

The structure of Insights Into the Role of Nucleotide-Dependent Conformational Change in Nitrogenase Catalysis: Structural Characterization of the Nitrogenase Fe Protein LEU127 Deletion Variant with Bound Mgatp also contains other interesting chemical elements:

Iron (Fe) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Insights Into the Role of Nucleotide-Dependent Conformational Change in Nitrogenase Catalysis: Structural Characterization of the Nitrogenase Fe Protein LEU127 Deletion Variant with Bound Mgatp (pdb code 2c8v). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Insights Into the Role of Nucleotide-Dependent Conformational Change in Nitrogenase Catalysis: Structural Characterization of the Nitrogenase Fe Protein LEU127 Deletion Variant with Bound Mgatp, PDB code: 2c8v:

Magnesium binding site 1 out of 1 in 2c8v

Go back to Magnesium Binding Sites List in 2c8v
Magnesium binding site 1 out of 1 in the Insights Into the Role of Nucleotide-Dependent Conformational Change in Nitrogenase Catalysis: Structural Characterization of the Nitrogenase Fe Protein LEU127 Deletion Variant with Bound Mgatp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Insights Into the Role of Nucleotide-Dependent Conformational Change in Nitrogenase Catalysis: Structural Characterization of the Nitrogenase Fe Protein LEU127 Deletion Variant with Bound Mgatp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg293

b:29.4
occ:1.00
 O1B A:ATP5292 2.2 31.9 1.0
OG A:SER16 2.3 12.0 1.0
O A:HOH2004 2.3 25.9 1.0
O A:HOH2099 2.4 53.7 1.0
O3G A:ATP5292 2.4 33.6 1.0
O A:HOH2014 2.4 46.3 1.0
O3B A:ATP5292 3.2 32.3 1.0
PB A:ATP5292 3.2 25.1 1.0
PG A:ATP5292 3.2 30.4 1.0
CB A:SER16 3.4 15.7 1.0
O2G A:ATP5292 3.8 37.2 1.0
N A:SER16 3.9 12.9 1.0
OD2 A:ASP43 3.9 35.2 1.0
OD1 A:ASP43 4.0 34.5 1.0
OD2 A:ASP125 4.1 26.8 1.0
CA A:SER16 4.2 14.6 1.0
O1A A:ATP5292 4.2 40.7 1.0
O2B A:ATP5292 4.3 34.6 1.0
O3A A:ATP5292 4.3 30.5 1.0
CG A:ASP43 4.3 36.7 1.0
OD2 A:ASP39 4.5 49.4 1.0
O2A A:ATP5292 4.5 39.9 1.0
PA A:ATP5292 4.6 30.8 1.0
O1G A:ATP5292 4.6 34.6 1.0
CB A:LYS15 4.8 17.0 1.0
NZ A:LYS41 4.8 50.8 1.0
C A:LYS15 4.8 13.2 1.0
CG A:ASP125 4.9 29.8 1.0
OD1 A:ASP125 4.9 30.9 1.0
CE A:LYS15 5.0 21.2 1.0

Reference:

S.Sen, A.Krishnakumar, J.Mcclead, M.K.Johnson, L.C.Seefeldt, R.K.Szilagyi, J.W.Peters. Insights Into the Role of Nucleotide-Dependent Conformational Change in Nitrogenase Catalysis: Structural Characterization of the Nitrogenase Fe Protein LEU127 Deletion Variant with Bound Mgatp. J.Inorg.Biochem. V. 100 1041 2006.
ISSN: ISSN 0162-0134
PubMed: 16616373
DOI: 10.1016/J.JINORGBIO.2006.02.016
Page generated: Sun Aug 10 10:15:04 2025

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