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Mercury in PDB 3f2f: Crystal Structure of the Mercury-Bound Form of Merb, the Organomercurial Lyase Involved in A Bacterial Mercury Resistance System

Enzymatic activity of Crystal Structure of the Mercury-Bound Form of Merb, the Organomercurial Lyase Involved in A Bacterial Mercury Resistance System

All present enzymatic activity of Crystal Structure of the Mercury-Bound Form of Merb, the Organomercurial Lyase Involved in A Bacterial Mercury Resistance System:
4.99.1.2;

Protein crystallography data

The structure of Crystal Structure of the Mercury-Bound Form of Merb, the Organomercurial Lyase Involved in A Bacterial Mercury Resistance System, PDB code: 3f2f was solved by J.Lafrance-Vanasse, M.Lefebvre, P.Di Lello, J.Sygusch, J.G.Omichinski, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.38 / 1.98
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 38.108, 88.836, 51.584, 90.00, 100.56, 90.00
R / Rfree (%) 17.3 / 21.7

Other elements in 3f2f:

The structure of Crystal Structure of the Mercury-Bound Form of Merb, the Organomercurial Lyase Involved in A Bacterial Mercury Resistance System also contains other interesting chemical elements:

Bromine (Br) 1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the Crystal Structure of the Mercury-Bound Form of Merb, the Organomercurial Lyase Involved in A Bacterial Mercury Resistance System (pdb code 3f2f). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 2 binding sites of Mercury where determined in the Crystal Structure of the Mercury-Bound Form of Merb, the Organomercurial Lyase Involved in A Bacterial Mercury Resistance System, PDB code: 3f2f:
Jump to Mercury binding site number: 1; 2;

Mercury binding site 1 out of 2 in 3f2f

Go back to Mercury Binding Sites List in 3f2f
Mercury binding site 1 out of 2 in the Crystal Structure of the Mercury-Bound Form of Merb, the Organomercurial Lyase Involved in A Bacterial Mercury Resistance System


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Crystal Structure of the Mercury-Bound Form of Merb, the Organomercurial Lyase Involved in A Bacterial Mercury Resistance System within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg213

b:17.3
occ:0.47
SG A:CYS96 2.4 12.0 1.0
SG A:CYS159 2.5 24.6 1.0
O A:HOH312 2.5 20.6 1.0
OD2 A:ASP99 2.9 18.7 1.0
OD1 A:ASP99 3.1 23.6 1.0
CG A:ASP99 3.2 19.7 1.0
CB A:CYS96 3.4 9.2 1.0
O A:HOH285 3.5 29.3 1.0
CB A:CYS159 3.6 11.2 1.0
CD2 A:PHE158 3.8 17.3 1.0
CE2 A:PHE158 3.9 15.4 1.0
CA A:CYS159 3.9 14.7 1.0
N A:CYS96 4.2 7.5 1.0
CB A:TRP95 4.4 10.8 1.0
CA A:CYS96 4.4 8.9 1.0
N A:CYS159 4.5 12.9 1.0
CB A:ASP99 4.5 9.6 1.0
C A:TRP95 4.5 10.5 1.0
N A:ASP99 4.8 7.4 1.0
O A:TRP95 4.9 8.6 1.0

Mercury binding site 2 out of 2 in 3f2f

Go back to Mercury Binding Sites List in 3f2f
Mercury binding site 2 out of 2 in the Crystal Structure of the Mercury-Bound Form of Merb, the Organomercurial Lyase Involved in A Bacterial Mercury Resistance System


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 2 of Crystal Structure of the Mercury-Bound Form of Merb, the Organomercurial Lyase Involved in A Bacterial Mercury Resistance System within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Hg213

b:20.4
occ:0.49
SG B:CYS96 2.4 11.7 1.0
SG B:CYS159 2.4 26.1 1.0
O B:HOH220 2.6 25.9 1.0
OD2 B:ASP99 3.0 19.3 1.0
CB B:CYS96 3.3 8.2 1.0
OD1 B:ASP99 3.4 22.0 1.0
O B:HOH245 3.4 21.0 1.0
CG B:ASP99 3.4 14.9 1.0
O B:HOH257 3.4 33.0 1.0
CB B:CYS159 3.5 15.3 1.0
CD2 B:PHE158 3.8 16.9 1.0
CA B:CYS159 3.8 14.4 1.0
CE2 B:PHE158 3.9 17.7 1.0
N B:CYS96 4.2 9.0 1.0
CA B:CYS96 4.4 12.3 1.0
N B:CYS159 4.4 12.4 1.0
CB B:TRP95 4.4 9.1 1.0
CB B:ASP99 4.6 11.5 1.0
C B:TRP95 4.6 7.8 1.0
N B:ASP99 4.9 10.0 1.0

Reference:

J.Lafrance-Vanasse, M.Lefebvre, P.Di Lello, J.Sygusch, J.G.Omichinski. Crystal Structures of the Organomercurial Lyase Merb in Its Free and Mercury-Bound Forms: Insights Into the Mechanism of Methylmercury Degradation J.Biol.Chem. V. 284 938 2009.
ISSN: ISSN 0021-9258
PubMed: 19004822
DOI: 10.1074/JBC.M807143200
Page generated: Sun Aug 11 03:42:21 2024

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