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Mercury in PDB 1hea: Carbonic Anhydrase II (Carbonate Dehydratase) (Hca II) (E.C.4.2.1.1) Mutant with Leu 198 Replaced By Arg (L198R)

Enzymatic activity of Carbonic Anhydrase II (Carbonate Dehydratase) (Hca II) (E.C.4.2.1.1) Mutant with Leu 198 Replaced By Arg (L198R)

All present enzymatic activity of Carbonic Anhydrase II (Carbonate Dehydratase) (Hca II) (E.C.4.2.1.1) Mutant with Leu 198 Replaced By Arg (L198R):
4.2.1.1;

Protein crystallography data

The structure of Carbonic Anhydrase II (Carbonate Dehydratase) (Hca II) (E.C.4.2.1.1) Mutant with Leu 198 Replaced By Arg (L198R), PDB code: 1hea was solved by S.K.Nair, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 2.00
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 1hea:

The structure of Carbonic Anhydrase II (Carbonate Dehydratase) (Hca II) (E.C.4.2.1.1) Mutant with Leu 198 Replaced By Arg (L198R) also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the Carbonic Anhydrase II (Carbonate Dehydratase) (Hca II) (E.C.4.2.1.1) Mutant with Leu 198 Replaced By Arg (L198R) (pdb code 1hea). 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 Carbonic Anhydrase II (Carbonate Dehydratase) (Hca II) (E.C.4.2.1.1) Mutant with Leu 198 Replaced By Arg (L198R), PDB code: 1hea:

Mercury binding site 1 out of 1 in 1hea

Go back to Mercury Binding Sites List in 1hea
Mercury binding site 1 out of 1 in the Carbonic Anhydrase II (Carbonate Dehydratase) (Hca II) (E.C.4.2.1.1) Mutant with Leu 198 Replaced By Arg (L198R)


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Carbonic Anhydrase II (Carbonate Dehydratase) (Hca II) (E.C.4.2.1.1) Mutant with Leu 198 Replaced By Arg (L198R) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg263

b:17.3
occ:1.00
SG A:CYS206 2.1 8.4 1.0
O A:GLN137 2.9 9.6 1.0
CB A:CYS206 3.0 7.5 1.0
C A:GLN137 3.4 9.9 1.0
O A:GLU205 3.5 7.8 1.0
CA A:CYS206 3.6 7.2 1.0
N A:GLN137 3.6 10.3 1.0
C A:GLU205 3.7 7.9 1.0
N A:CYS206 3.7 7.7 1.0
O A:VAL135 3.8 11.1 1.0
C A:GLN136 3.9 11.0 1.0
CA A:GLN137 4.0 10.0 1.0
C A:VAL135 4.1 11.4 1.0
N A:PRO138 4.1 9.8 1.0
O A:HOH301 4.2 3.4 1.0
N A:GLN136 4.3 11.2 1.0
CA A:GLN136 4.3 11.2 1.0
CA A:PRO138 4.4 9.7 1.0
O A:GLN136 4.4 10.3 1.0
N A:GLU205 4.5 7.8 1.0
CA A:GLU205 4.6 7.5 1.0
O A:HOH319 4.6 10.4 1.0
CA A:VAL135 4.8 11.6 1.0
O A:ALA134 4.9 12.0 1.0
CB A:LEU204 4.9 8.1 1.0
C A:CYS206 5.0 6.2 1.0
C A:LEU204 5.0 7.6 1.0

Reference:

S.K.Nair, D.W.Christianson. Structural Consequences of Hydrophilic Amino Acid Substitutions in the Hydrophobic Pocket of Human Carbonic Anhydrase II. Biochemistry V. 32 4506 1993.
ISSN: ISSN 0006-2960
PubMed: 8485129
DOI: 10.1021/BI00068A005
Page generated: Sun Dec 13 19:03:00 2020

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