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Mercury in PDB 5thj: Crystal Structure of 2-Hydroxycyclohepta-2,4,6-Trien-1-One Bound to Human Carbonic Anhydrase 2

Enzymatic activity of Crystal Structure of 2-Hydroxycyclohepta-2,4,6-Trien-1-One Bound to Human Carbonic Anhydrase 2

All present enzymatic activity of Crystal Structure of 2-Hydroxycyclohepta-2,4,6-Trien-1-One Bound to Human Carbonic Anhydrase 2:
4.2.1.1;

Protein crystallography data

The structure of Crystal Structure of 2-Hydroxycyclohepta-2,4,6-Trien-1-One Bound to Human Carbonic Anhydrase 2, PDB code: 5thj was solved by B.Dick, S.Cohen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.00 / 1.50
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.283, 41.340, 71.848, 90.00, 104.00, 90.00
R / Rfree (%) 15.4 / 18.9

Other elements in 5thj:

The structure of Crystal Structure of 2-Hydroxycyclohepta-2,4,6-Trien-1-One Bound to Human Carbonic Anhydrase 2 also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the Crystal Structure of 2-Hydroxycyclohepta-2,4,6-Trien-1-One Bound to Human Carbonic Anhydrase 2 (pdb code 5thj). 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 Crystal Structure of 2-Hydroxycyclohepta-2,4,6-Trien-1-One Bound to Human Carbonic Anhydrase 2, PDB code: 5thj:

Mercury binding site 1 out of 1 in 5thj

Go back to Mercury Binding Sites List in 5thj
Mercury binding site 1 out of 1 in the Crystal Structure of 2-Hydroxycyclohepta-2,4,6-Trien-1-One Bound to Human Carbonic Anhydrase 2


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Crystal Structure of 2-Hydroxycyclohepta-2,4,6-Trien-1-One Bound to Human Carbonic Anhydrase 2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg303

b:11.2
occ:0.80
 HG A:MBO303 0.0 11.2 0.8
CE1 A:MBO303 2.3 13.2 0.8
SG A:CYS206 2.3 11.5 1.0
O A:GLN137 3.0 8.1 1.0
CE2 A:MBO303 3.0 14.2 0.8
O A:VAL135 3.1 8.4 1.0
CE6 A:MBO303 3.1 9.6 0.8
CB A:CYS206 3.3 7.5 1.0
CA A:CYS206 3.6 6.7 1.0
N A:GLN137 3.6 7.7 1.0
C A:GLN137 3.6 8.2 1.0
O A:GLU205 3.6 8.3 1.0
C A:VAL135 3.6 8.6 1.0
N A:CYS206 3.7 6.4 1.0
C A:GLU205 3.7 7.0 1.0
N A:GLU205 4.0 6.1 1.0
C A:GLN136 4.0 8.8 1.0
O A:HOH569 4.0 20.4 1.0
CB A:LEU204 4.1 10.8 1.0
CA A:GLN137 4.2 7.9 1.0
N A:GLN136 4.2 8.8 1.0
CA A:GLN136 4.3 10.2 1.0
CE3 A:MBO303 4.3 14.2 0.8
CA A:VAL135 4.4 7.8 1.0
CA A:GLU205 4.4 7.1 1.0
C A:LEU204 4.4 6.9 1.0
CE5 A:MBO303 4.4 12.7 0.8
N A:PRO138 4.4 8.2 1.0
CA A:PRO138 4.7 7.9 1.0
O A:ALA134 4.7 7.9 1.0
CA A:LEU204 4.8 8.0 1.0
O A:GLN136 4.8 10.0 1.0
CE4 A:MBO303 4.8 14.2 0.8
O A:LEU204 4.9 6.6 1.0

Reference:

B.L.Dick, A.Patel, J.A.Mccammon, S.M.Cohen. Effect of Donor Atom Identity on Metal-Binding Pharmacophore Coordination. J. Biol. Inorg. Chem. V. 22 605 2017.
ISSN: ESSN 1432-1327
PubMed: 28389830
DOI: 10.1007/S00775-017-1454-3
Page generated: Sun Dec 13 19:13:12 2020

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