Mercury in PDB 1if5: Carbonic Anhydrase II Complexed with 2,6-Difluorobenzenesulfonamide

Enzymatic activity of Carbonic Anhydrase II Complexed with 2,6-Difluorobenzenesulfonamide

All present enzymatic activity of Carbonic Anhydrase II Complexed with 2,6-Difluorobenzenesulfonamide:
4.2.1.1;

Protein crystallography data

The structure of Carbonic Anhydrase II Complexed with 2,6-Difluorobenzenesulfonamide, PDB code: 1if5 was solved by C.-Y.Kim, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	20.00 / 2.00
*Space group*	P 1 2₁ 1
*Cell size a, b, c (Å), α, β, γ (°)*	43.200, 42.700, 73.300, 90.00, 104.58, 90.00
*R / R_free (%)*	22.1 / 28.7

Other elements in 1if5:

The structure of Carbonic Anhydrase II Complexed with 2,6-Difluorobenzenesulfonamide also contains other interesting chemical elements:

Fluorine	(F)	2 atoms
Zinc	(Zn)	1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the Carbonic Anhydrase II Complexed with 2,6-Difluorobenzenesulfonamide (pdb code 1if5). 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 Complexed with 2,6-Difluorobenzenesulfonamide, PDB code: 1if5:

Mercury binding site 1 out of 1 in 1if5

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Mercury Binding Sites List in 1if5

Mercury binding site 1 out of 1 in the Carbonic Anhydrase II Complexed with 2,6-Difluorobenzenesulfonamide

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 Complexed with 2,6-Difluorobenzenesulfonamide within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Hg263 b:20.2 occ:1.00	SG	A:CYS206	1.6	23.5	1.0
	CB	A:CYS206	2.8	14.6	1.0
	O	A:GLN137	3.2	14.4	1.0
	O	A:VAL135	3.3	19.9	1.0
	CA	A:CYS206	3.4	13.0	1.0
	O	A:GLU205	3.5	9.8	1.0
	N	A:CYS206	3.6	9.0	1.0
	C	A:GLU205	3.6	9.3	1.0
	C	A:GLN137	3.6	16.9	1.0
	N	A:GLN137	3.7	19.0	1.0
	C	A:VAL135	3.9	18.9	1.0
	C	A:GLN136	4.0	18.4	1.0
	O	A:HOH310	4.0	41.0	1.0
	O	A:HOH322	4.1	20.4	1.0
	CA	A:GLN137	4.2	18.8	1.0
	CA	A:GLN136	4.3	18.4	1.0
	N	A:PRO138	4.3	16.8	1.0
	N	A:GLU205	4.3	8.2	1.0
	N	A:GLN136	4.4	16.7	1.0
	O	A:GLN136	4.5	19.1	1.0
	O	A:HOH280	4.5	20.2	1.0
	CA	A:GLU205	4.5	7.7	1.0
	CA	A:PRO138	4.6	15.4	1.0
	CB	A:LEU204	4.6	10.0	1.0
	CA	A:VAL135	4.8	17.1	1.0
	C	A:LEU204	4.8	9.2	1.0
	C	A:CYS206	4.9	10.9	1.0
	O	A:ALA134	5.0	17.4	1.0

Reference:

C.-Y.Kim, D.W.Christianson. Binding of Fluorine Substituted Benzenesulfonamides to Carbonic Anhydrase II To Be Published.

Page generated: Sun Dec 13 19:03:10 2020

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