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Mercury in PDB 3zp9: Human Carbonic Anhydrase II As A Scaffold For An Artificial Transfer Hydrogenase

Enzymatic activity of Human Carbonic Anhydrase II As A Scaffold For An Artificial Transfer Hydrogenase

All present enzymatic activity of Human Carbonic Anhydrase II As A Scaffold For An Artificial Transfer Hydrogenase:
4.2.1.1;

Protein crystallography data

The structure of Human Carbonic Anhydrase II As A Scaffold For An Artificial Transfer Hydrogenase, PDB code: 3zp9 was solved by T.Heinisch, T.Schirmer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.011 / 1.31
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.500, 41.620, 72.480, 90.00, 103.80, 90.00
R / Rfree (%) 16.83 / 19.32

Other elements in 3zp9:

The structure of Human Carbonic Anhydrase II As A Scaffold For An Artificial Transfer Hydrogenase also contains other interesting chemical elements:

Zinc (Zn) 1 atom
Iridium (Ir) 1 atom
Chlorine (Cl) 1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the Human Carbonic Anhydrase II As A Scaffold For An Artificial Transfer Hydrogenase (pdb code 3zp9). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total only one binding site of Mercury was determined in the Human Carbonic Anhydrase II As A Scaffold For An Artificial Transfer Hydrogenase, PDB code: 3zp9:

Mercury binding site 1 out of 1 in 3zp9

Go back to Mercury Binding Sites List in 3zp9
Mercury binding site 1 out of 1 in the Human Carbonic Anhydrase II As A Scaffold For An Artificial Transfer Hydrogenase


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Human Carbonic Anhydrase II As A Scaffold For An Artificial Transfer Hydrogenase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg1006

b:14.5
occ:0.60
HG A:MBO1006 0.0 14.5 0.6
CE1 A:MBO1006 2.3 14.3 0.6
SG A:CYS206 2.3 19.8 1.0
O A:GLN137 2.9 13.7 1.0
O A:HOH2101 3.0 23.9 1.0
CE2 A:MBO1006 3.1 14.8 0.6
O A:GLU205 3.2 14.3 1.0
CE6 A:MBO1006 3.2 14.4 0.6
CB A:CYS206 3.3 12.0 1.0
C A:GLN137 3.3 12.2 1.0
C A:GLU205 3.5 10.2 1.0
CA A:CYS206 3.5 12.1 1.0
N A:GLN137 3.6 16.0 1.0
N A:CYS206 3.7 12.0 1.0
O A:HOH2141 3.7 23.3 1.0
N A:PRO138 4.0 13.2 1.0
CA A:GLN137 4.0 15.6 1.0
CA A:PRO138 4.0 13.0 1.0
O A:VAL135 4.0 26.6 1.0
C A:GLN136 4.1 13.9 1.0
N A:GLU205 4.2 12.9 1.0
CA A:GLU205 4.4 13.4 1.0
C A:VAL135 4.4 15.9 1.0
CE3 A:MBO1006 4.5 14.8 0.6
CE5 A:MBO1006 4.5 14.6 0.6
CA A:GLN136 4.6 17.7 1.0
O A:GLN136 4.7 18.0 1.0
N A:GLN136 4.9 14.5 1.0
C A:LEU204 4.9 12.4 1.0
CB A:LEU204 4.9 17.6 1.0
C A:CYS206 4.9 14.9 1.0
CE4 A:MBO1006 5.0 14.9 0.6
CD A:PRO138 5.0 20.0 1.0

Reference:

F.W.Monnard, E.S.Nogueira, T.Heinisch, T.Schirmer, T.R.Ward. Human Carbonic Anhydrase II As Host Protein For the Creation of Artificial Metalloenzymes: the Asymmetric Transfer Hydrogenation of Imines Chem.Sci. V. 4 3269 2013.
ISSN: ISSN 2041-6520
DOI: 10.1039/C3SC51065D
Page generated: Sun Dec 13 19:10:40 2020

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