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Magnesium in PDB 1s4m: Crystal Structure of Flavin Binding to Fad Synthetase From Thermotoga Maritina

Protein crystallography data

The structure of Crystal Structure of Flavin Binding to Fad Synthetase From Thermotoga Maritina, PDB code: 1s4m was solved by W.Wang, R.Kim, H.Yokota, S.-H.Kim, Berkeley Structural Genomics Center(Bsgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.10
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 66.093, 82.163, 66.754, 90.00, 116.57, 90.00
R / Rfree (%) 21.2 / 25.9

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Flavin Binding to Fad Synthetase From Thermotoga Maritina (pdb code 1s4m). 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 Flavin Binding to Fad Synthetase From Thermotoga Maritina, PDB code: 1s4m:

Magnesium binding site 1 out of 1 in 1s4m

Go back to Magnesium Binding Sites List in 1s4m
Magnesium binding site 1 out of 1 in the Crystal Structure of Flavin Binding to Fad Synthetase From Thermotoga Maritina


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 Flavin Binding to Fad Synthetase From Thermotoga Maritina within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg295

b:36.5
occ:1.00
O A:HOH741 2.2 37.6 1.0
O A:HOH738 2.2 36.7 1.0
O A:HOH739 2.3 40.2 1.0
O A:HOH740 2.4 76.4 1.0
O A:GLY119 2.5 40.1 1.0
C A:GLY119 3.5 40.1 1.0
CA A:GLY119 4.0 39.7 1.0
O A:SER94 4.5 33.6 1.0
N A:VAL120 4.6 37.9 1.0
O A:HOH646 4.7 39.2 1.0
OE2 A:GLU121 4.7 45.3 1.0
CG A:GLU121 4.7 40.6 1.0
CA A:VAL120 4.8 37.4 1.0
N A:GLU121 4.9 33.6 1.0
CB A:SER94 4.9 34.4 1.0

Reference:

W.Wang, R.Kim, H.Yokota, S.-H.Kim. Crystal Structure of Flavin Binding to Fad Synthetase of Thermotoga Maritima Proteins V. 58 246 2005.
ISSN: ISSN 0887-3585
PubMed: 15468322
DOI: 10.1002/PROT.20207
Page generated: Tue Aug 13 13:15:24 2024

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