Atomistry » Mercury » PDB 1is9-1obh » 1nu9
Atomistry »
  Mercury »
    PDB 1is9-1obh »
      1nu9 »

Mercury in PDB 1nu9: Staphylocoagulase-Prethrombin-2 Complex

Enzymatic activity of Staphylocoagulase-Prethrombin-2 Complex

All present enzymatic activity of Staphylocoagulase-Prethrombin-2 Complex:
3.4.21.5;

Protein crystallography data

The structure of Staphylocoagulase-Prethrombin-2 Complex, PDB code: 1nu9 was solved by R.Friedrich, W.Bode, P.Fuentes-Prior, P.Panizzi, P.E.Bock, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.98 / 2.20
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 181.160, 102.340, 135.540, 90.00, 129.91, 90.00
R / Rfree (%) 21 / 25.3

Mercury Binding Sites:

The binding sites of Mercury atom in the Staphylocoagulase-Prethrombin-2 Complex (pdb code 1nu9). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 4 binding sites of Mercury where determined in the Staphylocoagulase-Prethrombin-2 Complex, PDB code: 1nu9:
Jump to Mercury binding site number: 1; 2; 3; 4;

Mercury binding site 1 out of 4 in 1nu9

Go back to Mercury Binding Sites List in 1nu9
Mercury binding site 1 out of 4 in the Staphylocoagulase-Prethrombin-2 Complex


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Staphylocoagulase-Prethrombin-2 Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Hg999

b:53.2
occ:0.60
S2 A:0ZJ299 2.6 52.8 1.0
OD2 C:ASP106 2.9 48.3 1.0
C2 A:0ZJ299 3.2 42.1 1.0
HG C:HG996 3.4 53.8 0.4
CG C:ASP106 3.4 48.0 1.0
C1 A:0ZJ299 4.0 42.8 1.0
OD1 C:ASP106 4.0 51.8 1.0
O2 A:0ZJ299 4.1 40.1 1.0
CB C:ASP106 4.2 44.6 1.0
O A:HOH391 4.8 43.5 1.0

Mercury binding site 2 out of 4 in 1nu9

Go back to Mercury Binding Sites List in 1nu9
Mercury binding site 2 out of 4 in the Staphylocoagulase-Prethrombin-2 Complex


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 2 of Staphylocoagulase-Prethrombin-2 Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Hg996

b:53.8
occ:0.40
S2 A:0ZJ299 2.3 52.8 1.0
O A:HOH391 2.8 43.5 1.0
O A:HOH378 3.0 41.4 1.0
OD1 C:ASP106 3.2 51.8 1.0
HG C:HG999 3.4 53.2 0.6
CG C:ASP106 3.8 48.0 1.0
C2 A:0ZJ299 3.8 42.1 1.0
OD2 C:ASP106 4.0 48.3 1.0
C1 A:0ZJ299 4.0 42.8 1.0
CA A:GLU217 4.1 33.5 1.0
N A:0ZJ299 4.1 39.9 1.0
CB A:GLU217 4.1 35.4 1.0
CG A:GLU217 4.3 37.8 1.0
N A:GLY219 4.3 35.3 1.0
C A:GLU217 4.6 34.3 1.0
O2 A:0ZJ299 4.7 40.1 1.0
O C:HOH2143 4.9 42.4 1.0
O A:HOH384 4.9 55.1 1.0
O A:GLY216 4.9 33.5 1.0
CB A:0ZJ299 4.9 40.3 1.0
CB C:ASP106 4.9 44.6 1.0
NH2 A:ARG221 5.0 42.6 1.0
CA A:0ZJ299 5.0 39.0 1.0

Mercury binding site 3 out of 4 in 1nu9

Go back to Mercury Binding Sites List in 1nu9
Mercury binding site 3 out of 4 in the Staphylocoagulase-Prethrombin-2 Complex


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 3 of Staphylocoagulase-Prethrombin-2 Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Hg998

b:54.5
occ:0.60
S2 D:0ZJ299 2.5 49.4 1.0
C2 D:0ZJ299 3.1 44.5 1.0
HG F:HG997 3.3 55.2 0.4
OD1 F:ASP106 3.5 52.7 1.0
CG F:ASP106 3.5 48.8 1.0
OD2 F:ASP106 3.5 48.4 1.0
C1 D:0ZJ299 3.9 44.5 1.0
O2 D:0ZJ299 3.9 44.6 1.0
CB F:ASP106 4.2 45.6 1.0
N D:0ZJ299 5.0 41.6 1.0

Mercury binding site 4 out of 4 in 1nu9

Go back to Mercury Binding Sites List in 1nu9
Mercury binding site 4 out of 4 in the Staphylocoagulase-Prethrombin-2 Complex


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 4 of Staphylocoagulase-Prethrombin-2 Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Hg997

b:55.2
occ:0.40
S2 D:0ZJ299 2.2 49.4 1.0
O D:HOH389 2.9 46.0 1.0
OD1 F:ASP106 2.9 52.7 1.0
O D:HOH384 3.3 43.8 1.0
HG F:HG998 3.3 54.5 0.6
C2 D:0ZJ299 3.7 44.5 1.0
C1 D:0ZJ299 3.9 44.5 1.0
CG F:ASP106 3.9 48.8 1.0
N D:0ZJ299 4.1 41.6 1.0
CA D:GLU217 4.1 36.8 1.0
OD2 F:ASP106 4.2 48.4 1.0
CG D:GLU217 4.2 40.0 1.0
CB D:GLU217 4.2 37.9 1.0
N D:GLY219 4.3 36.0 1.0
O2 D:0ZJ299 4.4 44.6 1.0
C D:GLU217 4.7 36.9 1.0
NH2 D:ARG221 4.7 39.5 1.0
O F:HOH2225 4.8 52.3 1.0
O D:GLY216 4.8 38.2 1.0
CB D:0ZJ299 4.8 42.0 1.0
CA D:0ZJ299 4.9 40.5 1.0

Reference:

R.Friedrich, P.Panizzi, P.Fuentes-Prior, K.Richter, I.Verhamme, P.J.Anderson, S.Kawabata, R.Huber, W.Bode, P.E.Bock. Staphylocoagulase Is A Prototype For the Mechanism of Cofactor-Induced Zymogen Activation Nature V. 425 535 2003.
ISSN: ISSN 0028-0836
PubMed: 14523451
DOI: 10.1038/NATURE01962
Page generated: Sun Aug 11 00:42:35 2024

Last articles

Ca in 5TPK
Ca in 5TS2
Ca in 5TR2
Ca in 5TRQ
Ca in 5TRX
Ca in 5TQG
Ca in 5TQF
Ca in 5TQE
Ca in 5TNC
Ca in 5TP9
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy