Mercury in PDB 1cny: Secondary Interactions Significantly Removed From the Sulfonamide Binding Pocket of Carbonic Anhydrase II Influence Binding Constants

Enzymatic activity of Secondary Interactions Significantly Removed From the Sulfonamide Binding Pocket of Carbonic Anhydrase II Influence Binding Constants

All present enzymatic activity of Secondary Interactions Significantly Removed From the Sulfonamide Binding Pocket of Carbonic Anhydrase II Influence Binding Constants:
4.2.1.1;

Protein crystallography data

The structure of Secondary Interactions Significantly Removed From the Sulfonamide Binding Pocket of Carbonic Anhydrase II Influence Binding Constants, PDB code: 1cny was solved by P.A.Boriack, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	N/A / 2.30
*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 / R_free (%)*	n/a / n/a

Other elements in 1cny:

The structure of Secondary Interactions Significantly Removed From the Sulfonamide Binding Pocket of Carbonic Anhydrase II Influence Binding Constants also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the Secondary Interactions Significantly Removed From the Sulfonamide Binding Pocket of Carbonic Anhydrase II Influence Binding Constants (pdb code 1cny). 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 Secondary Interactions Significantly Removed From the Sulfonamide Binding Pocket of Carbonic Anhydrase II Influence Binding Constants, PDB code: 1cny:

Mercury binding site 1 out of 1 in 1cny

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Mercury Binding Sites List in 1cny

Mercury binding site 1 out of 1 in the Secondary Interactions Significantly Removed From the Sulfonamide Binding Pocket of Carbonic Anhydrase II Influence Binding Constants

Mono view

Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Secondary Interactions Significantly Removed From the Sulfonamide Binding Pocket of Carbonic Anhydrase II Influence Binding Constants within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Hg362 b:19.1 occ:1.00	CB	A:CYS206	2.9	11.1	1.0
	SG	A:CYS206	3.0	14.2	1.0
	O	A:GLN137	3.1	11.9	1.0
	C	A:GLN137	3.4	12.2	1.0
	O	A:HOH363	3.4	8.7	1.0
	O	A:GLU205	3.5	7.6	1.0
	CA	A:CYS206	3.6	9.5	1.0
	N	A:GLN137	3.6	13.0	1.0
	C	A:GLU205	3.6	8.2	1.0
	O	A:VAL135	3.6	13.6	1.0
	N	A:CYS206	3.7	8.7	1.0
	C	A:GLN136	3.7	13.3	1.0
	N	A:PRO138	4.0	11.6	1.0
	CA	A:GLN137	4.0	12.6	1.0
	O	A:GLN136	4.1	13.3	1.0
	C	A:VAL135	4.1	13.3	1.0
	O	A:HOH331	4.1	5.7	1.0
	CA	A:GLN136	4.2	13.7	1.0
	O	A:HOH365	4.3	15.6	1.0
	CA	A:PRO138	4.3	11.1	1.0
	N	A:GLN136	4.4	13.3	1.0
	N	A:GLU205	4.5	8.1	1.0
	CA	A:GLU205	4.6	8.0	1.0
	CD	A:PRO138	4.9	11.6	1.0
	CB	A:LEU204	4.9	7.5	1.0
	C	A:LEU204	4.9	8.1	1.0
	CA	A:VAL135	5.0	13.3	1.0
	O	A:ALA134	5.0	13.2	1.0

Reference:

P.A.Boriack, D.W.Christianson, J.Kingery-Wood, G.M.Whitesides. Secondary Interactions Significantly Removed From the Sulfonamide Binding Pocket of Carbonic Anhydrase II Influence Inhibitor Binding Constants. J.Med.Chem. V. 38 2286 1995.
ISSN: ISSN 0022-2623
PubMed: 7608893
DOI: 10.1021/JM00013A004

Page generated: Sat Aug 10 23:24:46 2024

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