Mercury in PDB 3t5u: Crystal Structure of the Human Carbonic Anhydrase II in Complex with N-Hydroxy Benzenesulfonamide

Enzymatic activity of Crystal Structure of the Human Carbonic Anhydrase II in Complex with N-Hydroxy Benzenesulfonamide

All present enzymatic activity of Crystal Structure of the Human Carbonic Anhydrase II in Complex with N-Hydroxy Benzenesulfonamide:
4.2.1.1;

Protein crystallography data

The structure of Crystal Structure of the Human Carbonic Anhydrase II in Complex with N-Hydroxy Benzenesulfonamide, PDB code: 3t5u was solved by A.Di Fiore, A.Maresca, V.Alterio, C.T.Supuran, G.De Simone, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	20.00 / 1.75
*Space group*	P 1 2₁ 1
*Cell size a, b, c (Å), α, β, γ (°)*	42.260, 41.540, 72.090, 90.00, 104.43, 90.00
*R / R_free (%)*	17.1 / 18.3

Other elements in 3t5u:

The structure of Crystal Structure of the Human Carbonic Anhydrase II in Complex with N-Hydroxy Benzenesulfonamide also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the Crystal Structure of the Human Carbonic Anhydrase II in Complex with N-Hydroxy Benzenesulfonamide (pdb code 3t5u). 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 Crystal Structure of the Human Carbonic Anhydrase II in Complex with N-Hydroxy Benzenesulfonamide, PDB code: 3t5u:

Mercury binding site 1 out of 1 in 3t5u

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Mercury Binding Sites List in 3t5u

Mercury binding site 1 out of 1 in the Crystal Structure of the Human Carbonic Anhydrase II in Complex with N-Hydroxy Benzenesulfonamide

Mono view

Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Crystal Structure of the Human Carbonic Anhydrase II in Complex with N-Hydroxy Benzenesulfonamide within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Hg268 b:17.3 occ:1.00	HG	A:MBO268	0.0	17.3	1.0
	CE1	A:MBO268	2.0	18.7	1.0
	SG	A:CYS206	2.3	16.8	1.0
	O	A:HOH373	2.7	20.0	1.0
	O	A:GLN137	2.9	12.8	1.0
	CE2	A:MBO268	3.0	19.1	1.0
	CE6	A:MBO268	3.0	19.3	1.0
	O	A:GLU205	3.1	9.4	1.0
	CB	A:CYS206	3.2	11.6	1.0
	C	A:GLN137	3.4	12.9	1.0
	C	A:GLU205	3.4	10.7	1.0
	CA	A:CYS206	3.5	10.5	1.0
	N	A:CYS206	3.6	10.3	1.0
	O	A:HOH322	3.8	16.6	1.0
	N	A:GLN137	3.8	13.1	1.0
	N	A:PRO138	3.9	12.6	1.0
	O	A:VAL135	4.0	14.5	1.0
	C	A:GLN136	4.1	13.2	1.0
	CA	A:PRO138	4.1	11.8	1.0
	CA	A:GLN137	4.1	11.4	1.0
	N	A:GLU205	4.3	7.3	1.0
	CE3	A:MBO268	4.3	19.5	1.0
	CE5	A:MBO268	4.3	18.1	1.0
	CA	A:GLU205	4.4	7.5	1.0
	C	A:VAL135	4.4	14.2	1.0
	CA	A:GLN136	4.5	14.6	1.0
	O	A:GLN136	4.6	13.9	1.0
	N	A:GLN136	4.6	13.8	1.0
	O	A:HOH444	4.7	33.3	1.0
	CE4	A:MBO268	4.9	17.9	1.0
	C	A:LEU204	4.9	8.4	1.0
	CD	A:PRO138	5.0	14.1	1.0
	CB	A:LEU204	5.0	8.9	1.0
	CB	A:GLU205	5.0	9.3	1.0
	C	A:CYS206	5.0	10.3	1.0

Reference:

A.Di Fiore, A.Maresca, V.Alterio, C.T.Supuran, G.De Simone. Carbonic Anhydrase Inhibitors: X-Ray Crystallographic Studies For the Binding of N-Substituted Benzenesulfonamides to Human Isoform II. Chem.Commun.(Camb.) V. 47 11636 2011.
ISSN: ISSN 1359-7345
PubMed: 21952494
DOI: 10.1039/C1CC14575D

Page generated: Sun Aug 11 04:09:25 2024

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