Mercury in PDB 1b5t: Escherichia Coli Methylenetetrahydrofolate Reductase

All present enzymatic activity of Escherichia Coli Methylenetetrahydrofolate Reductase:
1.7.99.5;

The structure of Escherichia Coli Methylenetetrahydrofolate Reductase, PDB code: 1b5t was solved by B.D.Guenther, C.A.Sheppard, P.Tran, R.Rozen, R.G.Matthews, M.L.Ludwig, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.50
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	103.000, 128.200, 98.200, 90.00, 121.60, 90.00
R / Rfree (%)	21.2 / 26.3

The binding sites of Mercury atom in the Escherichia Coli Methylenetetrahydrofolate Reductase (pdb code 1b5t). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 3 binding sites of Mercury where determined in the Escherichia Coli Methylenetetrahydrofolate Reductase, PDB code: 1b5t:
Jump to Mercury binding site number: 1; 2; 3;

Mercury binding site 1 out of 3 in the Escherichia Coli Methylenetetrahydrofolate Reductase


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Escherichia Coli Methylenetetrahydrofolate Reductase within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg501 b:45.4 occ:0.90 CB A:CYS91 1.8 23.4 1.0 SG A:CYS91 2.7 25.1 1.0 CA A:CYS91 3.2 23.3 1.0 O A:MET130 3.4 23.2 1.0 C A:CYS91 3.5 25.0 1.0 CG A:ARG118 3.7 16.9 1.0 O A:ARG118 3.8 17.4 1.0 N A:ILE92 3.8 24.9 1.0 CB A:MET130 3.9 27.5 1.0 N A:CYS91 3.9 21.3 1.0 O A:CYS91 3.9 27.7 1.0 C A:MET130 4.0 25.0 1.0 CG A:MET130 4.3 29.9 1.0 CD A:ARG118 4.3 20.3 1.0 CA A:ARG118 4.5 15.7 1.0 C A:ARG118 4.5 16.8 1.0 SD A:MET130 4.5 34.8 1.0 CA A:MET130 4.5 27.5 1.0 CD1 A:ILE92 4.5 18.9 1.0 CB A:ARG118 4.7 16.4 1.0 CA A:ILE92 4.7 25.4 1.0 N A:TYR131 4.8 20.9 1.0 N A:MET130 5.0 32.5 1.0

Mercury binding site 2 out of 3 in the Escherichia Coli Methylenetetrahydrofolate Reductase


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 2 of Escherichia Coli Methylenetetrahydrofolate Reductase within 5.0Å range: probe atom residue distance (Å) B Occ B:Hg501 b:44.2 occ:0.90 SG B:CYS91 2.5 26.8 1.0 C B:CYS91 3.3 28.4 1.0 CB B:CYS91 3.3 25.0 1.0 N B:ILE92 3.4 31.1 1.0 O B:MET130 3.5 27.9 1.0 O B:CYS91 3.5 28.9 1.0 CB B:MET130 3.7 35.0 1.0 CA B:CYS91 3.7 26.8 1.0 O B:ARG118 3.9 23.0 1.0 CA B:ILE92 3.9 32.4 1.0 C B:MET130 3.9 28.3 1.0 CD B:ARG118 4.0 20.0 1.0 CG B:ARG118 4.2 19.2 1.0 CG B:MET130 4.2 36.9 1.0 N B:CYS91 4.3 24.1 1.0 SD B:MET130 4.4 38.7 1.0 CA B:MET130 4.4 32.8 1.0 N B:TYR131 4.6 23.7 1.0 C B:ARG118 4.6 21.4 1.0 CA B:ARG118 4.6 18.6 1.0 CD1 B:ILE92 4.6 34.0 1.0 O B:ILE92 4.7 38.2 1.0 C B:ILE92 4.7 34.6 1.0 N B:MET130 4.9 36.8 1.0 CA B:TYR131 4.9 20.1 1.0

Mercury binding site 3 out of 3 in the Escherichia Coli Methylenetetrahydrofolate Reductase


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 3 of Escherichia Coli Methylenetetrahydrofolate Reductase within 5.0Å range: probe atom residue distance (Å) B Occ C:Hg501 b:30.8 occ:0.30 SG C:CYS91 1.9 50.6 1.0 CB C:CYS91 2.7 49.3 1.0 C C:CYS91 2.8 51.3 1.0 N C:ILE92 2.9 53.5 1.0 O C:CYS91 3.1 52.5 1.0 CA C:CYS91 3.3 50.0 1.0 CA C:ILE92 3.4 54.1 1.0 CG C:ARG118 3.7 37.0 1.0 O C:ARG118 3.7 40.4 1.0 CB C:ILE92 4.0 54.8 1.0 N C:CYS91 4.1 46.8 1.0 CD C:ARG118 4.2 37.2 1.0 C C:ARG118 4.4 39.9 1.0 CA C:ARG118 4.5 37.6 1.0 N C:TYR131 4.5 46.0 1.0 CB C:ARG118 4.7 38.3 1.0 C C:ILE92 4.8 53.8 1.0 CA C:TYR131 4.9 45.9 1.0 CG1 C:ILE92 4.9 55.5 1.0

B.D.Guenther, C.A.Sheppard, P.Tran, R.Rozen, R.G.Matthews, M.L.Ludwig. The Structure and Properties of Methylenetetrahydrofolate Reductase From Escherichia Coli Suggest How Folate Ameliorates Human Hyperhomocysteinemia. Nat.Struct.Biol. V. 6 359 1999.
ISSN: ISSN 1072-8368
PubMed: 10201405
DOI: 10.1038/7594