Mercury in PDB 4fl7: The Crystal Structure of Human Carbonic Anhydrase II in Complex with N-(Hydroxy)-Benzamide

Enzymatic activity of The Crystal Structure of Human Carbonic Anhydrase II in Complex with N-(Hydroxy)-Benzamide

All present enzymatic activity of The Crystal Structure of Human Carbonic Anhydrase II in Complex with N-(Hydroxy)-Benzamide:
4.2.1.1;

Protein crystallography data

The structure of The Crystal Structure of Human Carbonic Anhydrase II in Complex with N-(Hydroxy)-Benzamide, PDB code: 4fl7 was solved by A.Di Fiore, G.De Simone, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	20.00 / 1.85
*Space group*	P 1 2₁ 1
*Cell size a, b, c (Å), α, β, γ (°)*	42.160, 41.500, 71.990, 90.00, 104.39, 90.00
*R / R_free (%)*	16.3 / 20.3

Other elements in 4fl7:

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

Zinc

(Zn)

1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the The Crystal Structure of Human Carbonic Anhydrase II in Complex with N-(Hydroxy)-Benzamide (pdb code 4fl7). 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 The Crystal Structure of Human Carbonic Anhydrase II in Complex with N-(Hydroxy)-Benzamide, PDB code: 4fl7:

Mercury binding site 1 out of 1 in 4fl7

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Mercury Binding Sites List in 4fl7

Mercury binding site 1 out of 1 in the The Crystal Structure of Human Carbonic Anhydrase II in Complex with N-(Hydroxy)-Benzamide

Mono view

Stereo pair view

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

probe	atom	residue	distance (Å)	B	Occ
A:Hg305 b:15.5 occ:0.80	HG	A:MBO305	0.0	15.5	0.8
	SG	A:CYS206	2.1	13.0	1.0
	CE1	A:MBO305	2.1	16.1	0.8
	O	A:GLN137	2.8	4.8	1.0
	O	A:HOH536	3.0	26.8	1.0
	CB	A:CYS206	3.0	10.8	1.0
	CE6	A:MBO305	3.1	15.4	0.8
	CE2	A:MBO305	3.1	14.7	0.8
	O	A:GLU205	3.3	7.0	1.0
	C	A:GLN137	3.4	7.9	1.0
	CA	A:CYS206	3.4	7.9	1.0
	C	A:GLU205	3.5	7.6	1.0
	N	A:CYS206	3.6	8.2	1.0
	N	A:GLN137	3.7	9.2	1.0
	O	A:VAL135	3.8	6.4	1.0
	N	A:PRO138	4.0	8.2	1.0
	O	A:HOH499	4.1	17.1	1.0
	C	A:GLN136	4.1	10.7	1.0
	CA	A:GLN137	4.1	7.1	1.0
	CA	A:PRO138	4.2	7.4	1.0
	C	A:VAL135	4.2	9.2	1.0
	N	A:GLU205	4.3	4.9	1.0
	CE5	A:MBO305	4.4	15.4	0.8
	CE3	A:MBO305	4.5	16.5	0.8
	CA	A:GLU205	4.5	6.0	1.0
	CA	A:GLN136	4.5	11.8	1.0
	N	A:GLN136	4.6	9.0	1.0
	O	A:GLN136	4.7	10.2	1.0
	CB	A:LEU204	4.8	6.1	1.0
	C	A:LEU204	4.9	5.6	1.0
	C	A:CYS206	4.9	7.0	1.0
	CE4	A:MBO305	5.0	15.0	0.8

Reference:

A.Di Fiore, A.Maresca, C.T.Supuran, G.De Simone. Hydroxamate Represents A Versatile Zinc Binding Group For the Development of New Carbonic Anhydrase Inhibitors. Chem.Commun.(Camb.) V. 48 8838 2012.
ISSN: ISSN 1359-7345
PubMed: 22836518
DOI: 10.1039/C2CC34275H

Page generated: Sun Aug 11 04:38:11 2024

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