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Mercury in PDB 1ptk: Studies on the Inhibitory Action of Mercury Upon Proteinase K

Enzymatic activity of Studies on the Inhibitory Action of Mercury Upon Proteinase K

All present enzymatic activity of Studies on the Inhibitory Action of Mercury Upon Proteinase K:
3.4.21.64;

Protein crystallography data

The structure of Studies on the Inhibitory Action of Mercury Upon Proteinase K, PDB code: 1ptk was solved by A.Mueller, W.Saenger, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 2.40
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 68.360, 68.360, 108.410, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Other elements in 1ptk:

The structure of Studies on the Inhibitory Action of Mercury Upon Proteinase K also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the Studies on the Inhibitory Action of Mercury Upon Proteinase K (pdb code 1ptk). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 3 binding sites of Mercury where determined in the Studies on the Inhibitory Action of Mercury Upon Proteinase K, PDB code: 1ptk:
Jump to Mercury binding site number: 1; 2; 3;

Mercury binding site 1 out of 3 in 1ptk

Go back to Mercury Binding Sites List in 1ptk
Mercury binding site 1 out of 3 in the Studies on the Inhibitory Action of Mercury Upon Proteinase K


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Studies on the Inhibitory Action of Mercury Upon Proteinase K within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg280

b:23.1
occ:1.00
SG A:CYS73 2.4 13.4 1.0
ND1 A:HIS69 2.9 29.8 1.0
O A:HIS69 3.0 20.1 1.0
OD2 A:ASP39 3.0 19.6 1.0
CB A:CYS73 3.2 5.0 1.0
CG A:HIS69 3.3 7.6 1.0
CE1 A:HIS69 3.3 21.9 1.0
OD1 A:ASP39 3.3 13.5 1.0
C A:HIS69 3.4 12.8 1.0
CG A:ASP39 3.5 5.0 1.0
NE2 A:HIS69 3.8 33.7 1.0
CD2 A:HIS69 3.8 43.5 1.0
OG A:SER224 3.8 21.5 0.7
CB A:HIS69 3.8 18.3 1.0
CB A:SER132 3.9 5.0 1.0
N A:GLY70 4.0 6.9 1.0
HG A:HG282 4.0 34.5 0.3
CA A:HIS69 4.1 5.0 1.0
CA A:GLY70 4.2 7.2 1.0
N A:CYS73 4.2 5.0 1.0
CA A:CYS73 4.3 5.0 1.0
OG A:SER132 4.3 19.1 1.0
O A:SER132 4.5 24.1 1.0
O A:SER224 4.6 10.8 1.0
CE A:MET225 4.7 5.0 1.0
CB A:SER224 4.8 15.4 1.0
CB A:ASP39 4.8 12.8 1.0
C A:GLY70 4.9 14.1 1.0
O A:HOH471 5.0 45.8 1.0

Mercury binding site 2 out of 3 in 1ptk

Go back to Mercury Binding Sites List in 1ptk
Mercury binding site 2 out of 3 in the Studies on the Inhibitory Action of Mercury Upon Proteinase K


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 2 of Studies on the Inhibitory Action of Mercury Upon Proteinase K within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg282

b:34.5
occ:0.30
HG A:HG282 0.0 34.5 0.3
ND1 A:HIS72 2.4 10.6 1.0
HG A:HG282 2.5 48.5 0.2
SG A:CYS73 2.9 13.4 1.0
N A:CYS73 3.0 5.0 1.0
CE A:MET225 3.1 5.0 1.0
CG A:HIS72 3.2 9.0 1.0
CB A:HIS72 3.3 5.0 1.0
C A:HIS72 3.3 5.0 1.0
CA A:CYS73 3.3 5.0 1.0
CE1 A:HIS72 3.6 5.0 1.0
O A:HIS72 3.7 5.0 1.0
CB A:CYS73 3.8 5.0 1.0
CA A:HIS72 3.9 5.9 1.0
O A:HIS69 3.9 20.1 1.0
HG A:HG280 4.0 23.1 1.0
CG A:MET225 4.1 11.3 1.0
O A:SER224 4.3 10.8 1.0
CA A:MET225 4.3 5.0 1.0
CD1 A:ILE220 4.4 31.1 1.0
SD A:MET225 4.4 13.8 1.0
CD2 A:HIS72 4.5 5.0 1.0
NE2 A:HIS72 4.6 5.0 1.0
C A:CYS73 4.7 5.0 1.0
C A:SER224 4.7 14.5 1.0
CG A:PRO228 4.7 5.0 1.0
N A:MET225 4.7 7.9 1.0
CB A:MET225 4.7 5.0 1.0
CG1 A:ILE220 4.8 27.9 1.0
OG1 A:THR76 4.9 12.3 1.0
N A:HIS72 4.9 5.2 1.0
C A:HIS69 4.9 12.8 1.0

Mercury binding site 3 out of 3 in 1ptk

Go back to Mercury Binding Sites List in 1ptk
Mercury binding site 3 out of 3 in the Studies on the Inhibitory Action of Mercury Upon Proteinase K


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 3 of Studies on the Inhibitory Action of Mercury Upon Proteinase K within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg282

b:48.5
occ:0.25
HG A:HG282 0.0 48.5 0.2
HG A:HG282 2.5 34.5 0.3
OG1 A:THR76 2.6 12.3 1.0
ND1 A:HIS72 3.1 10.6 1.0
CB A:THR76 3.2 5.8 1.0
CE1 A:HIS72 3.5 5.0 1.0
O A:HIS72 3.6 5.0 1.0
CA A:MET225 3.7 5.0 1.0
CG A:PRO228 3.7 5.0 1.0
O A:MET225 3.8 6.2 1.0
CG2 A:THR76 3.9 8.8 1.0
CA A:CYS73 3.9 5.0 1.0
C A:HIS72 4.0 5.0 1.0
CG A:MET225 4.0 11.3 1.0
CB A:MET225 4.0 5.0 1.0
CG2 A:ILE208 4.2 5.0 1.0
N A:CYS73 4.2 5.0 1.0
C A:MET225 4.2 12.9 1.0
CG A:HIS72 4.2 9.0 1.0
SG A:CYS73 4.3 13.4 1.0
O A:CYS73 4.5 8.4 1.0
CA A:THR76 4.6 6.8 1.0
CE A:MET225 4.6 5.0 1.0
O A:SER224 4.6 10.8 1.0
CB A:PRO228 4.7 5.0 1.0
N A:THR76 4.7 5.0 1.0
CB A:SER210 4.7 13.9 1.0
C A:CYS73 4.7 5.0 1.0
NE2 A:HIS72 4.7 5.0 1.0
N A:MET225 4.8 7.9 1.0
CB A:ILE208 4.8 5.0 1.0
CB A:CYS73 4.8 5.0 1.0
CB A:HIS72 4.8 5.0 1.0
OG A:SER210 4.8 5.0 1.0
CD A:PRO228 4.9 5.0 1.0
CA A:HIS72 5.0 5.9 1.0

Reference:

A.Muller, W.Saenger. Studies on the Inhibitory Action of Mercury Upon Proteinase K. J.Biol.Chem. V. 268 26150 1993.
ISSN: ISSN 0021-9258
PubMed: 8253733
Page generated: Sun Dec 13 19:04:43 2020

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