Mercury in PDB 4awb: Crystal Structure of Active Legumain in Complex with Aan-Cmk

All present enzymatic activity of Crystal Structure of Active Legumain in Complex with Aan-Cmk:
3.4.22.34;

The structure of Crystal Structure of Active Legumain in Complex with Aan-Cmk, PDB code: 4awb was solved by E.Dall, H.Brandstetter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	63.91 / 2.70
Space group	P 41
Cell size a, b, c (Å), α, β, γ (°)	63.900, 63.900, 144.390, 90.00, 90.00, 90.00
R / Rfree (%)	22.933 / 25.506

The binding sites of Mercury atom in the Crystal Structure of Active Legumain in Complex with Aan-Cmk (pdb code 4awb). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 4 binding sites of Mercury where determined in the Crystal Structure of Active Legumain in Complex with Aan-Cmk, PDB code: 4awb:
Jump to Mercury binding site number: 1; 2; 3; 4;

Mercury binding site 1 out of 4 in the Crystal Structure of Active Legumain in Complex with Aan-Cmk


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 Active Legumain in Complex with Aan-Cmk within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg325 b:80.8 occ:1.00 SG A:CYS219 2.1 34.2 1.0 OH A:TYR220 3.1 36.7 1.0 CZ A:TYR220 3.2 37.1 1.0 CG1 A:VAL235 3.3 34.7 1.0 CZ3 A:TRP232 3.3 35.6 1.0 CE2 A:TYR220 3.6 37.0 1.0 CE3 A:TRP232 3.7 35.5 1.0 CB A:CYS219 3.7 35.6 1.0 CH2 A:TRP232 3.7 35.6 1.0 CE1 A:TYR220 3.8 37.0 1.0 CB A:VAL235 4.1 34.2 1.0 CD2 A:TYR220 4.4 37.0 1.0 CD2 A:TRP232 4.4 35.4 1.0 CZ2 A:TRP232 4.5 35.5 1.0 CD1 A:TYR220 4.5 37.1 1.0 OD1 A:ASN236 4.7 35.3 1.0 CG2 A:VAL235 4.7 34.1 1.0 CE2 A:TRP232 4.7 35.5 1.0 CG A:TYR220 4.8 37.1 1.0 CA A:CYS219 4.9 36.4 1.0 OE1 A:GLU239 5.0 34.1 1.0

Mercury binding site 2 out of 4 in the Crystal Structure of Active Legumain in Complex with Aan-Cmk


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 Active Legumain in Complex with Aan-Cmk within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg326 b:92.6 occ:1.00 NE2 A:HIS162 2.4 42.9 1.0 CD2 A:HIS162 3.2 42.5 1.0 O B:PRO157 3.2 28.4 1.0 OD1 B:ASN38 3.4 36.0 1.0 CE1 A:HIS162 3.4 42.4 1.0 CD1 A:ILE153 3.8 33.6 1.0 C B:PRO157 4.1 28.3 1.0 CG1 A:ILE153 4.2 33.6 1.0 CG A:HIS162 4.4 41.9 1.0 O A:HOH2028 4.4 35.7 1.0 ND1 A:HIS162 4.4 42.1 1.0 CA B:PRO157 4.5 27.8 1.0 CG B:ASN38 4.5 36.0 1.0 O B:PHE156 4.5 26.9 1.0 OD2 A:ASP160 4.7 41.4 1.0 ND2 B:ASN38 4.8 36.1 1.0

Mercury binding site 3 out of 4 in the Crystal Structure of Active Legumain in Complex with Aan-Cmk


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 Active Legumain in Complex with Aan-Cmk within 5.0Å range: probe atom residue distance (Å) B Occ B:Hg325 b:98.1 occ:1.00 SG B:CYS219 2.2 35.9 1.0 CZ3 B:TRP232 3.3 46.2 1.0 OH B:TYR220 3.5 40.0 1.0 CZ B:TYR220 3.6 40.0 1.0 CE3 B:TRP232 3.6 45.7 1.0 CG1 B:VAL235 3.9 41.6 1.0 CH2 B:TRP232 3.9 45.9 1.0 CE2 B:TYR220 3.9 40.0 1.0 CB B:CYS219 4.0 38.6 1.0 CE1 B:TYR220 4.0 40.1 1.0 CD2 B:TRP232 4.4 45.5 1.0 CB B:VAL235 4.6 41.8 1.0 CD2 B:TYR220 4.6 40.1 1.0 CD1 B:TYR220 4.7 40.1 1.0 CZ2 B:TRP232 4.7 45.8 1.0 CE2 B:TRP232 4.9 45.6 1.0 CG B:TYR220 5.0 40.2 1.0

Mercury binding site 4 out of 4 in the Crystal Structure of Active Legumain in Complex with Aan-Cmk


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 4 of Crystal Structure of Active Legumain in Complex with Aan-Cmk within 5.0Å range: probe atom residue distance (Å) B Occ B:Hg326 b:0.2 occ:1.00 NE2 B:HIS162 2.4 33.4 1.0 CE1 B:HIS162 3.3 33.3 1.0 CD2 B:HIS162 3.5 32.7 1.0 O A:PRO157 3.7 38.3 1.0 O A:PHE156 3.8 35.1 1.0 O A:HOH2026 3.9 38.3 1.0 CD1 B:ILE153 4.0 26.6 1.0 CA A:PRO157 4.1 37.1 1.0 C A:PRO157 4.2 38.2 1.0 OD1 A:ASN38 4.2 31.2 1.0 CG1 A:VAL155 4.4 32.7 1.0 ND1 B:HIS162 4.5 32.7 1.0 CG1 B:ILE153 4.5 26.6 1.0 CG B:HIS162 4.6 32.5 1.0 C A:PHE156 4.7 35.3 1.0 N A:PRO157 4.9 36.1 1.0 O A:GLY36 4.9 31.0 1.0

E.Dall, H.Brandstetter. Mechanistic and Structural Studies on Legumain Explain Its Zymogenicity, Distinct Activation Pathways, and Regulation Proc.Natl.Acad.Sci.Usa V. 110 10940 2013.
ISSN: ISSN 0027-8424
PubMed: 23776206
DOI: 10.1073/PNAS.1300686110