Atomistry » Mercury » PDB 1of5-1rsr » 1ptk
Atomistry »
  Mercury »
    PDB 1of5-1rsr »
      1ptk »

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: Wed Oct 28 18:40:25 2020

Last articles

Xe in 6AYK
Xe in 6QII
Xe in 6ASM
Xe in 5NSW
Xe in 6FY9
Xe in 5O1K
Xe in 5O27
Xe in 5M69
Xe in 5KPU
Xe in 5I63
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy