Mercury in PDB 1rwa: Crystal Structure of Arthrobacter Aurescens Chondroitin Ac Lyase

All present enzymatic activity of Crystal Structure of Arthrobacter Aurescens Chondroitin Ac Lyase:
4.2.2.5;

The structure of Crystal Structure of Arthrobacter Aurescens Chondroitin Ac Lyase, PDB code: 1rwa was solved by V.V.Lunin, Y.Li, H.Miyazono, M.Kyogashima, A.W.Bell, M.Cygler, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.99 / 1.30
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	57.356, 85.256, 82.162, 90.00, 105.78, 90.00
R / Rfree (%)	13.4 / 15.6

The binding sites of Mercury atom in the Crystal Structure of Arthrobacter Aurescens Chondroitin Ac Lyase (pdb code 1rwa). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 3 binding sites of Mercury where determined in the Crystal Structure of Arthrobacter Aurescens Chondroitin Ac Lyase, PDB code: 1rwa:
Jump to Mercury binding site number: 1; 2; 3;

Mercury binding site 1 out of 3 in the Crystal Structure of Arthrobacter Aurescens Chondroitin Ac Lyase


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 Arthrobacter Aurescens Chondroitin Ac Lyase within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg900 b:17.4 occ:0.90 O A:HOH1185 1.8 19.0 1.0 SG A:CYS408 2.3 13.9 1.0 O A:HOH1298 3.3 22.7 1.0 N A:CYS408 3.3 11.1 1.0 CB A:CYS408 3.3 10.9 1.0 CZ A:TYR406 3.4 9.7 1.0 CE1 A:TYR406 3.5 10.8 1.0 OH A:TYR406 3.5 12.2 1.0 O A:HOH1081 3.7 14.4 1.0 O A:HOH1665 3.8 30.5 1.0 CA A:CYS408 3.8 11.9 1.0 CE2 A:TYR406 4.0 9.1 1.0 O A:CYS408 4.0 11.8 1.0 O A:HOH1341 4.1 24.0 1.0 CD1 A:TYR406 4.1 10.1 1.0 C A:CYS408 4.2 11.1 1.0 C A:GLU407 4.3 9.8 1.0 O A:TYR406 4.5 9.8 1.0 CD2 A:TYR406 4.6 8.9 1.0 CA A:LYS460 4.6 11.4 1.0 CG A:TYR406 4.6 8.9 1.0 O A:VAL461 4.6 12.3 1.0 O A:LYS460 4.7 13.3 1.0 CA A:GLU407 4.7 9.2 1.0 C A:LYS460 4.8 10.8 1.0 C A:TYR406 5.0 8.8 1.0 O A:HOH1053 5.0 12.8 1.0

Mercury binding site 2 out of 3 in the Crystal Structure of Arthrobacter Aurescens Chondroitin Ac Lyase


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 Arthrobacter Aurescens Chondroitin Ac Lyase within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg901 b:22.4 occ:0.60 O A:HOH1556 2.2 28.7 1.0 SG A:CYS156 2.4 19.1 1.0 O A:HOH1666 2.9 31.5 1.0 CB A:CYS156 3.3 15.6 1.0 O A:ARG152 3.4 18.5 1.0 CA A:GLY198 3.5 16.4 1.0 O A:HOH1427 3.7 25.8 1.0 C A:ARG152 3.8 17.8 1.0 CB A:ARG152 4.0 18.4 1.0 N A:THR153 4.3 16.4 1.0 N A:GLY198 4.3 17.8 1.0 CA A:ARG152 4.4 19.1 1.0 CA A:THR153 4.5 17.1 1.0 CA A:CYS156 4.6 16.8 1.0 CG A:ARG152 4.6 23.0 1.0 NH1 A:ARG194 4.6 17.0 1.0 O A:ALA197 4.7 19.1 1.0 CE A:MET140 4.7 20.4 0.6 C A:ALA197 4.7 17.3 1.0 CD A:ARG152 4.7 22.5 1.0 N A:CYS156 4.7 16.1 1.0 C A:GLY198 4.8 17.1 1.0 O A:GLY198 5.0 19.8 1.0 CZ A:ARG194 5.0 17.2 1.0 NH2 A:ARG194 5.0 16.6 1.0

Mercury binding site 3 out of 3 in the Crystal Structure of Arthrobacter Aurescens Chondroitin Ac Lyase


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 3 of Crystal Structure of Arthrobacter Aurescens Chondroitin Ac Lyase within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg902 b:25.9 occ:0.40 SG A:CYS114 2.2 27.1 1.0 O A:HOH1823 2.2 35.7 1.0 O A:LEU66 3.1 28.9 1.0 O A:HOH1356 3.2 24.1 1.0 CB A:CYS114 3.2 20.9 1.0 O A:HOH1959 3.6 39.7 1.0 CH2 A:TRP128 3.7 21.1 1.0 CA A:CYS114 3.8 22.1 1.0 C A:LEU66 4.0 27.9 1.0 CZ2 A:TRP128 4.3 20.5 1.0 C A:CYS114 4.3 21.8 1.0 O A:CYS114 4.3 23.0 1.0 CE A:LYS119 4.4 36.4 1.0 SD A:MET72 4.4 20.9 1.0 CB A:LEU66 4.7 26.3 1.0 O A:HOH2019 4.7 42.0 1.0 CA A:ALA67 4.7 28.3 1.0 N A:ALA67 4.7 28.3 1.0 CZ3 A:TRP128 4.7 19.8 1.0 O A:HOH1619 4.7 29.9 1.0 NZ A:LYS119 4.8 39.7 1.0 CA A:LEU66 4.9 26.2 1.0

V.V.Lunin, Y.Li, R.J.Linhardt, H.Miyazono, M.Kyogashima, T.Kaneko, A.W.Bell, M.Cygler. High-Resolution Crystal Structure of Arthrobacter Aurescens Chondroitin Ac Lyase: An Enzyme-Substrate Complex Defines the Catalytic Mechanism J.Mol.Biol. V. 337 367 2004.
ISSN: ISSN 0022-2836
PubMed: 15003453
DOI: 10.1016/J.JMB.2003.12.071