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Mercury in PDB 1bv3: Human Carbonic Anhydrase II Complexed with Urea

Enzymatic activity of Human Carbonic Anhydrase II Complexed with Urea

All present enzymatic activity of Human Carbonic Anhydrase II Complexed with Urea:
4.2.1.1;

Protein crystallography data

The structure of Human Carbonic Anhydrase II Complexed with Urea, PDB code: 1bv3 was solved by F.Briganti, S.Mangani, A.Scozzafava, G.Vernaglione, C.T.Supuran, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.85
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.820, 42.020, 73.030, 90.00, 104.26, 90.00
R / Rfree (%) 17.1 / 21.3

Other elements in 1bv3:

The structure of Human Carbonic Anhydrase II Complexed with Urea also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the Human Carbonic Anhydrase II Complexed with Urea (pdb code 1bv3). 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 Complexed with Urea, PDB code: 1bv3:

Mercury binding site 1 out of 1 in 1bv3

Go back to Mercury Binding Sites List in 1bv3
Mercury binding site 1 out of 1 in the Human Carbonic Anhydrase II Complexed with Urea


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 Complexed with Urea within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg263

b:9.4
occ:1.00
HG A:HGB263 0.0 9.4 1.0
C7 A:HGB263 2.1 18.2 1.0
SG A:CYS206 2.2 4.5 1.0
O A:HOH390 2.9 38.1 1.0
O A:GLN137 3.0 2.1 1.0
C5 A:HGB263 3.1 17.7 1.0
C6 A:HGB263 3.1 16.2 1.0
CB A:CYS206 3.2 2.0 1.0
O A:GLU205 3.2 9.7 1.0
O A:HOH331 3.3 17.3 1.0
C A:GLN137 3.4 3.5 1.0
CA A:CYS206 3.5 6.5 1.0
C A:GLU205 3.7 2.0 1.0
N A:GLN137 3.7 4.3 1.0
O A:HOH357 3.8 17.2 1.0
N A:CYS206 3.9 3.0 1.0
N A:PRO138 3.9 2.8 1.0
C A:GLN136 4.1 6.4 1.0
CA A:GLN137 4.1 5.9 1.0
O A:VAL135 4.1 9.9 1.0
CA A:PRO138 4.2 3.2 1.0
C3 A:HGB263 4.4 18.5 1.0
C4 A:HGB263 4.4 15.9 1.0
O A:GLN136 4.4 7.5 1.0
N A:GLU205 4.4 2.0 1.0
CA A:GLU205 4.5 2.0 1.0
C A:VAL135 4.5 7.5 1.0
CA A:GLN136 4.6 6.8 1.0
N A:GLN136 4.8 3.2 1.0
C A:CYS206 5.0 3.8 1.0
CD A:PRO138 5.0 3.2 1.0

Reference:

F.Briganti, S.Mangani, A.Scozzafava, G.Vernaglione, C.T.Supuran. Carbonic Anhydrase Catalyzes Cyanamide Hydration to Urea: Is It Mimicking the Physiological Reaction? J.Biol.Inorg.Chem. V. 4 528 1999.
ISSN: ISSN 0949-8257
PubMed: 10550681
DOI: 10.1007/S007750050375
Page generated: Sun Dec 13 19:02:08 2020

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