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Magnesium in PDB 1gs6: Crystal Structure of M144A Mutant of Alcaligenes Xylosoxidans Nitrite Reductase

Enzymatic activity of Crystal Structure of M144A Mutant of Alcaligenes Xylosoxidans Nitrite Reductase

All present enzymatic activity of Crystal Structure of M144A Mutant of Alcaligenes Xylosoxidans Nitrite Reductase:
1.7.2.1; 1.7.99.3;

Protein crystallography data

The structure of Crystal Structure of M144A Mutant of Alcaligenes Xylosoxidans Nitrite Reductase, PDB code: 1gs6 was solved by M.J.Ellis, M.Prudencio, F.E.Dodd, R.W.Strange, G.Sawers, R.R.Eady, S.S.Hasnain, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 60.00 / 2.2
Space group P 63
Cell size a, b, c (Å), α, β, γ (°) 106.860, 106.860, 64.026, 90.00, 90.00, 120.00
R / Rfree (%) 14.8 / 18.1

Other elements in 1gs6:

The structure of Crystal Structure of M144A Mutant of Alcaligenes Xylosoxidans Nitrite Reductase also contains other interesting chemical elements:

Copper (Cu) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of M144A Mutant of Alcaligenes Xylosoxidans Nitrite Reductase (pdb code 1gs6). 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 Crystal Structure of M144A Mutant of Alcaligenes Xylosoxidans Nitrite Reductase, PDB code: 1gs6:

Magnesium binding site 1 out of 1 in 1gs6

Go back to Magnesium Binding Sites List in 1gs6
Magnesium binding site 1 out of 1 in the Crystal Structure of M144A Mutant of Alcaligenes Xylosoxidans Nitrite Reductase


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 M144A Mutant of Alcaligenes Xylosoxidans Nitrite Reductase within 5.0Å range:
probe atom residue distance (Å) B Occ
X:Mg1339

b:24.0
occ:1.00
OG X:SER281 2.8 10.9 1.0
O X:GLU260 2.9 16.5 1.0
N X:ARG278 3.0 12.9 1.0
NH1 X:ARG278 3.2 16.0 1.0
CD X:ARG278 3.4 15.4 1.0
CA X:THR261 3.6 17.5 1.0
CA X:ILE277 3.6 12.5 1.0
C X:GLU260 3.7 17.2 1.0
C X:ILE277 3.7 13.5 1.0
CG X:ARG278 3.8 16.1 1.0
CB X:ARG278 3.8 14.6 1.0
O X:PHE276 3.8 12.1 1.0
CB X:SER281 3.9 15.2 1.0
CA X:ARG278 4.0 13.5 1.0
N X:THR261 4.0 17.4 1.0
CZ X:ARG278 4.1 14.1 1.0
NE X:ARG278 4.2 15.1 1.0
C X:THR261 4.3 17.4 1.0
CG2 X:ILE277 4.4 14.0 1.0
O X:ARG278 4.4 12.6 1.0
CG2 X:THR261 4.5 20.4 1.0
CB X:ILE277 4.5 13.0 1.0
CB X:THR261 4.5 18.8 1.0
O X:THR261 4.5 16.2 1.0
N X:ILE277 4.6 12.3 1.0
C X:PHE276 4.6 13.1 1.0
CD1 X:ILE277 4.7 17.5 1.0
C X:ARG278 4.7 13.3 1.0
CA X:GLU260 5.0 17.0 1.0
O X:ALA282 5.0 16.7 1.0

Reference:

M.J.Ellis, M.Prudencio, F.E.Dodd, R.W.Strange, G.Sawers, R.R.Eady, S.S.Hasnain. Biochemical and Crystallographic Studies of the MET144ALA, ASP92ASN and HIS254PHE Mutants of the Nitrite Reductase From Alcaligenes Xylosoxidans Provide Insight Into the Enzyme Mechanism. J.Mol.Biol. V. 316 51 2002.
ISSN: ISSN 0022-2836
PubMed: 11829502
DOI: 10.1006/JMBI.2001.5304
Page generated: Mon Dec 14 05:58:20 2020

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