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Mercury in PDB 1bic: Crystallographic Analysis of Thr-200-> His Human Carbonic Anhydrase II and Its Complex with the Substrate, HCO3-

Enzymatic activity of Crystallographic Analysis of Thr-200-> His Human Carbonic Anhydrase II and Its Complex with the Substrate, HCO3-

All present enzymatic activity of Crystallographic Analysis of Thr-200-> His Human Carbonic Anhydrase II and Its Complex with the Substrate, HCO3-:
4.2.1.1;

Protein crystallography data

The structure of Crystallographic Analysis of Thr-200-> His Human Carbonic Anhydrase II and Its Complex with the Substrate, HCO3-, PDB code: 1bic was solved by Y.Xue, J.Vidgren, L.A.Svensson, A.Liljas, B.-H.Jonsson, S.Lindskog, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 1.90
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.700, 41.700, 73.000, 90.00, 104.60, 90.00
R / Rfree (%) n/a / n/a

Other elements in 1bic:

The structure of Crystallographic Analysis of Thr-200-> His Human Carbonic Anhydrase II and Its Complex with the Substrate, HCO3- also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the Crystallographic Analysis of Thr-200-> His Human Carbonic Anhydrase II and Its Complex with the Substrate, HCO3- (pdb code 1bic). 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 Crystallographic Analysis of Thr-200-> His Human Carbonic Anhydrase II and Its Complex with the Substrate, HCO3-, PDB code: 1bic:

Mercury binding site 1 out of 1 in 1bic

Go back to Mercury Binding Sites List in 1bic
Mercury binding site 1 out of 1 in the Crystallographic Analysis of Thr-200-> His Human Carbonic Anhydrase II and Its Complex with the Substrate, HCO3-


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Crystallographic Analysis of Thr-200-> His Human Carbonic Anhydrase II and Its Complex with the Substrate, HCO3- within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg500

b:9.9
occ:0.75
 HG A:MMC500 0.0 9.9 0.8
SG A:CYS206 1.8 2.0 0.8
C A:MMC500 2.0 6.8 0.8
O A:GLN137 3.0 9.7 1.0
SG A:CYS206 3.0 2.0 0.2
CB A:CYS206 3.1 4.9 0.8
C A:GLN137 3.3 10.0 1.0
CB A:CYS206 3.3 4.0 0.2
O A:GLU205 3.4 5.9 1.0
CA A:CYS206 3.5 4.4 1.0
N A:GLN137 3.5 10.9 1.0
O A:VAL135 3.6 12.2 1.0
C A:GLU205 3.8 6.1 1.0
C A:GLN136 3.8 11.0 1.0
N A:CYS206 3.9 5.1 1.0
CA A:GLN137 3.9 10.7 1.0
N A:PRO138 3.9 9.9 1.0
O A:HOH331 4.1 11.4 1.0
C A:VAL135 4.1 11.5 1.0
CA A:PRO138 4.3 9.9 1.0
CA A:GLN136 4.3 10.9 1.0
O A:GLN136 4.3 10.6 1.0
O A:HOH365 4.4 13.2 1.0
N A:GLN136 4.4 11.0 1.0
N A:GLU205 4.6 6.5 1.0
CA A:GLU205 4.7 6.0 1.0
CA A:VAL135 4.9 11.7 1.0
O A:ALA134 5.0 12.2 1.0
CD A:PRO138 5.0 10.6 1.0
CB A:LEU204 5.0 6.5 1.0
C A:CYS206 5.0 5.4 1.0

Reference:

Y.Xue, J.Vidgren, L.A.Svensson, A.Liljas, B.H.Jonsson, S.Lindskog. Crystallographic Analysis of Thr-200-->His Human Carbonic Anhydrase II and Its Complex with the Substrate, HCO3-. Proteins V. 15 80 1993.
ISSN: ISSN 0887-3585
PubMed: 8451242
DOI: 10.1002/PROT.340150110
Page generated: Sat Aug 10 23:19:17 2024

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