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Mercury in PDB 1moo: Site Specific Mutant (H64A) of Human Carbonic Anhydrase II at High Resolution

Enzymatic activity of Site Specific Mutant (H64A) of Human Carbonic Anhydrase II at High Resolution

All present enzymatic activity of Site Specific Mutant (H64A) of Human Carbonic Anhydrase II at High Resolution:
4.2.1.1;

Protein crystallography data

The structure of Site Specific Mutant (H64A) of Human Carbonic Anhydrase II at High Resolution, PDB code: 1moo was solved by D.M.Duda, L.Govindasamy, M.Agbandje-Mckenna, C.K.Tu, D.N.Silverman, R.Mckenna, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.05
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.188, 41.435, 72.041, 90.00, 104.26, 90.00
R / Rfree (%) 15.7 / 17.7

Other elements in 1moo:

The structure of Site Specific Mutant (H64A) of Human Carbonic Anhydrase II at High Resolution also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the Site Specific Mutant (H64A) of Human Carbonic Anhydrase II at High Resolution (pdb code 1moo). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 2 binding sites of Mercury where determined in the Site Specific Mutant (H64A) of Human Carbonic Anhydrase II at High Resolution, PDB code: 1moo:
Jump to Mercury binding site number: 1; 2;

Mercury binding site 1 out of 2 in 1moo

Go back to Mercury Binding Sites List in 1moo
Mercury binding site 1 out of 2 in the Site Specific Mutant (H64A) of Human Carbonic Anhydrase II at High Resolution


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Site Specific Mutant (H64A) of Human Carbonic Anhydrase II at High Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg263

b:14.0
occ:0.75
HG A:HG263 0.0 14.0 0.8
HG A:HG263 2.0 36.9 0.2
SG A:CYS206 2.3 11.0 0.7
O A:HOH421 2.4 28.9 1.0
O A:GLN137 2.9 8.2 1.0
CB A:CYS206 2.9 8.5 0.3
CB A:CYS206 3.1 9.8 0.7
O A:GLU205 3.2 10.8 1.0
C A:GLN137 3.4 8.3 1.0
O A:VAL135 3.4 18.1 1.0
CA A:CYS206 3.5 7.3 1.0
C A:GLU205 3.5 9.0 1.0
N A:GLN137 3.5 8.6 1.0
O A:HOH368 3.7 17.8 1.0
N A:CYS206 3.7 7.7 1.0
C A:GLN136 3.9 12.8 1.0
C A:VAL135 4.0 10.7 1.0
CA A:GLN137 4.1 8.2 1.0
N A:PRO138 4.1 10.0 1.0
SG A:CYS206 4.1 8.3 0.3
CA A:PRO138 4.2 9.6 1.0
O A:HOH496 4.3 36.9 1.0
N A:GLU205 4.3 7.7 1.0
CA A:GLN136 4.4 12.8 1.0
O A:HOH351 4.4 19.2 1.0
N A:GLN136 4.4 10.5 1.0
CA A:GLU205 4.5 7.5 1.0
O A:GLN136 4.5 12.5 1.0
CA A:VAL135 4.7 10.8 1.0
CB A:LEU204 4.7 9.5 1.0
O A:ALA134 4.9 9.1 1.0
C A:LEU204 4.9 7.5 1.0
C A:CYS206 4.9 6.8 1.0

Mercury binding site 2 out of 2 in 1moo

Go back to Mercury Binding Sites List in 1moo
Mercury binding site 2 out of 2 in the Site Specific Mutant (H64A) of Human Carbonic Anhydrase II at High Resolution


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 2 of Site Specific Mutant (H64A) of Human Carbonic Anhydrase II at High Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg263

b:36.9
occ:0.25
HG A:HG263 0.0 36.9 0.2
HG A:HG263 2.0 14.0 0.8
O A:HOH421 3.0 28.9 1.0
O A:HOH496 3.2 36.9 1.0
C A:GLN137 3.2 8.3 1.0
N A:PRO138 3.4 10.0 1.0
O A:GLN137 3.4 8.2 1.0
O A:HOH351 3.5 19.2 1.0
O A:GLU205 3.6 10.8 1.0
N A:GLN137 3.6 8.6 1.0
C A:GLN136 3.7 12.8 1.0
CA A:PRO138 3.7 9.6 1.0
O A:GLN136 3.8 12.5 1.0
CA A:GLN137 3.8 8.2 1.0
CD A:PRO138 4.0 13.0 1.0
O A:HOH368 4.0 17.8 1.0
SG A:CYS206 4.3 11.0 0.7
CB A:PRO138 4.4 12.0 1.0
O A:HOH489 4.4 29.7 1.0
C A:GLU205 4.4 9.0 1.0
CA A:GLN136 4.6 12.8 1.0
O A:VAL135 4.6 18.1 1.0
CB A:CYS206 4.6 8.5 0.3
CG A:PRO138 4.7 16.6 1.0
CA A:CYS206 4.9 7.3 1.0
CB A:CYS206 4.9 9.8 0.7

Reference:

D.Duda, L.Govindasamy, M.Agbandje-Mckenna, C.Tu, D.N.Silverman, R.Mckenna. The Refined Atomic Structure of Carbonic Anhydrase II at 1.05 A Resolution: Implications of Chemical Rescue of Proton Transfer. Acta Crystallogr.,Sect.D V. 59 93 2003.
ISSN: ISSN 0907-4449
PubMed: 12499545
DOI: 10.1107/S0907444902019455
Page generated: Wed Oct 28 18:40:02 2020

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