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Mercury in PDB 2bno: The Structure of Hydroxypropylphosphonic Acid Epoxidase From S. Wedmorenis.

Protein crystallography data

The structure of The Structure of Hydroxypropylphosphonic Acid Epoxidase From S. Wedmorenis., PDB code: 2bno was solved by K.Mcluskey, S.Cameron, W.N.Hunter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.90
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 86.430, 86.430, 221.853, 90.00, 90.00, 120.00
R / Rfree (%) 18.1 / 24.2

Other elements in 2bno:

The structure of The Structure of Hydroxypropylphosphonic Acid Epoxidase From S. Wedmorenis. also contains other interesting chemical elements:

Zinc (Zn) 2 atoms

Mercury Binding Sites:

The binding sites of Mercury atom in the The Structure of Hydroxypropylphosphonic Acid Epoxidase From S. Wedmorenis. (pdb code 2bno). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 4 binding sites of Mercury where determined in the The Structure of Hydroxypropylphosphonic Acid Epoxidase From S. Wedmorenis., PDB code: 2bno:
Jump to Mercury binding site number: 1; 2; 3; 4;

Mercury binding site 1 out of 4 in 2bno

Go back to Mercury Binding Sites List in 2bno
Mercury binding site 1 out of 4 in the The Structure of Hydroxypropylphosphonic Acid Epoxidase From S. Wedmorenis.


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of The Structure of Hydroxypropylphosphonic Acid Epoxidase From S. Wedmorenis. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg1199

b:32.3
occ:0.50
HG A:HG1200 1.8 36.1 0.2
O A:HOH2125 2.0 43.7 1.0
SG A:CYS107 2.3 29.6 1.0
O B:HOH2039 2.3 41.8 1.0
O B:VAL22 3.0 24.7 1.0
CB A:CYS107 3.2 23.6 1.0
O A:HOH2127 3.3 43.3 1.0
CB A:PRO91 3.6 52.0 1.0
O B:LYS23 3.9 32.0 1.0
O A:PRO91 3.9 49.5 1.0
CB B:LYS23 4.1 30.6 1.0
C A:PRO91 4.1 52.1 1.0
NH1 A:ARG110 4.2 23.1 1.0
C B:VAL22 4.2 26.4 1.0
C B:LYS23 4.3 30.4 1.0
CG A:PRO91 4.3 55.0 1.0
CA A:PRO91 4.5 52.3 1.0
O B:HOH2010 4.6 54.6 1.0
CA A:CYS107 4.6 23.0 1.0
CA B:LYS23 4.6 29.4 1.0
N A:ILE92 4.7 53.2 1.0
NH2 A:ARG110 4.7 28.3 1.0
N A:CYS107 4.8 24.9 1.0
N B:LYS23 4.9 26.3 1.0
CZ A:ARG110 5.0 36.2 1.0
C A:ILE92 5.0 55.6 1.0
CD A:PRO91 5.0 53.2 1.0

Mercury binding site 2 out of 4 in 2bno

Go back to Mercury Binding Sites List in 2bno
Mercury binding site 2 out of 4 in the The Structure of Hydroxypropylphosphonic Acid Epoxidase From S. Wedmorenis.


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 2 of The Structure of Hydroxypropylphosphonic Acid Epoxidase From S. Wedmorenis. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg1200

b:36.1
occ:0.25
HG A:HG1199 1.8 32.3 0.5
SG A:CYS107 2.2 29.6 1.0
O A:PRO91 2.8 49.5 1.0
CB A:CYS107 3.2 23.6 1.0
C A:PRO91 3.3 52.1 1.0
O B:HOH2039 3.4 41.8 1.0
O A:TYR105 3.6 35.5 1.0
N A:LEU93 3.6 56.6 1.0
O A:HOH2125 3.6 43.7 1.0
N A:ILE92 3.6 53.2 1.0
CA A:ILE92 3.6 54.5 1.0
C A:ILE92 3.7 55.6 1.0
N A:CYS107 3.8 24.9 1.0
CB A:PRO91 3.9 52.0 1.0
CB B:LYS23 4.0 30.6 1.0
CA A:CYS107 4.1 23.0 1.0
O B:LYS23 4.1 32.0 1.0
O B:VAL22 4.2 24.7 1.0
CA A:PRO91 4.2 52.3 1.0
O A:ILE92 4.3 55.7 1.0
C A:TYR105 4.4 31.8 1.0
CB A:LEU93 4.5 58.6 1.0
O A:HOH2127 4.6 43.3 1.0
CA A:LEU93 4.7 58.3 1.0
C A:ASN106 4.7 26.2 1.0
CB A:TYR105 4.8 33.5 1.0
C B:LYS23 4.8 30.4 1.0
CG B:LYS23 4.9 30.6 1.0
CG A:PRO91 4.9 55.0 1.0
CA B:LYS23 5.0 29.4 1.0
CA A:ASN106 5.0 27.1 1.0

Mercury binding site 3 out of 4 in 2bno

Go back to Mercury Binding Sites List in 2bno
Mercury binding site 3 out of 4 in the The Structure of Hydroxypropylphosphonic Acid Epoxidase From S. Wedmorenis.


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 3 of The Structure of Hydroxypropylphosphonic Acid Epoxidase From S. Wedmorenis. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Hg1199

b:29.0
occ:0.50
HG B:HG1200 1.8 41.9 0.2
SG B:CYS107 2.4 28.2 1.0
O A:HOH2033 2.4 50.4 1.0
O A:VAL22 3.2 31.3 1.0
CB B:CYS107 3.2 23.3 1.0
CB B:PRO91 3.5 48.9 1.0
O B:HOH2155 3.8 47.3 1.0
O A:LYS23 3.8 34.7 1.0
CB A:LYS23 4.1 32.6 1.0
C B:PRO91 4.1 46.8 1.0
O B:PRO91 4.1 43.8 1.0
NH1 B:ARG110 4.2 25.8 1.0
C A:LYS23 4.3 33.3 1.0
CG B:PRO91 4.4 56.2 1.0
C A:VAL22 4.4 29.2 1.0
CA B:PRO91 4.5 49.0 1.0
N B:ILE92 4.5 46.3 1.0
O A:HOH2011 4.6 45.9 1.0
CA B:CYS107 4.6 22.9 1.0
CA A:LYS23 4.7 31.9 1.0
NH2 B:ARG110 4.7 23.1 1.0
N B:LEU93 4.8 47.7 1.0
N B:CYS107 4.9 23.6 1.0
CA B:ILE92 4.9 47.5 1.0
C B:ILE92 4.9 47.8 1.0
CZ B:ARG110 5.0 35.4 1.0
N A:LYS23 5.0 29.0 1.0
CD B:PRO91 5.0 51.3 1.0

Mercury binding site 4 out of 4 in 2bno

Go back to Mercury Binding Sites List in 2bno
Mercury binding site 4 out of 4 in the The Structure of Hydroxypropylphosphonic Acid Epoxidase From S. Wedmorenis.


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 4 of The Structure of Hydroxypropylphosphonic Acid Epoxidase From S. Wedmorenis. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Hg1200

b:41.9
occ:0.25
HG B:HG1199 1.8 29.0 0.5
SG B:CYS107 2.2 28.2 1.0
O B:PRO91 2.9 43.8 1.0
CB B:CYS107 3.0 23.3 1.0
C B:PRO91 3.2 46.8 1.0
N B:ILE92 3.4 46.3 1.0
CA B:ILE92 3.5 47.5 1.0
O B:TYR105 3.6 34.6 1.0
N B:LEU93 3.6 47.7 1.0
N B:CYS107 3.6 23.6 1.0
CB B:PRO91 3.7 48.9 1.0
C B:ILE92 3.8 47.8 1.0
O A:HOH2033 3.9 50.4 1.0
CA B:CYS107 3.9 22.9 1.0
CA B:PRO91 4.1 49.0 1.0
CB A:LYS23 4.2 32.6 1.0
C B:TYR105 4.3 31.8 1.0
O A:LYS23 4.3 34.7 1.0
O A:VAL22 4.5 31.3 1.0
CB B:LEU93 4.6 47.3 1.0
C B:ASN106 4.6 26.4 1.0
O B:ILE92 4.6 47.1 1.0
CB B:TYR105 4.7 30.2 1.0
CA B:LEU93 4.7 47.8 1.0
CG B:PRO91 4.8 56.2 1.0
N B:PRO91 4.9 51.2 1.0
CA B:ASN106 4.9 26.1 1.0
O B:HOH2155 4.9 47.3 1.0
N B:ASN106 4.9 27.4 1.0

Reference:

K.Mcluskey, S.Cameron, F.Hammerschmidt, W.N.Hunter. Structure and Reactivity of Hydroxypropylphosphonic Acid Epoxidase in Fosfomycin Biosynthesis By A Cation- and Flavin-Dependent Mechanism. Proc.Natl.Acad.Sci.Usa V. 102 14221 2005.
ISSN: ISSN 0027-8424
PubMed: 16186494
DOI: 10.1073/PNAS.0504314102
Page generated: Wed Oct 28 18:41:17 2020

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