Mercury in PDB 5bnl: Deciphering the Mechanism of Carbonic Anhydrase Inhibition with Coumarins and Thiocoumarins

Enzymatic activity of Deciphering the Mechanism of Carbonic Anhydrase Inhibition with Coumarins and Thiocoumarins

All present enzymatic activity of Deciphering the Mechanism of Carbonic Anhydrase Inhibition with Coumarins and Thiocoumarins:
4.2.1.1;

Protein crystallography data

The structure of Deciphering the Mechanism of Carbonic Anhydrase Inhibition with Coumarins and Thiocoumarins, PDB code: 5bnl was solved by C.Temperini, A.Maresca, L.Pochet, B.Masereel, A.Scozzafava, C.T.Supuran, 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 (°)*	42.230, 41.500, 72.420, 90.00, 104.50, 90.00
*R / R_free (%)*	22.3 / 29.3

Other elements in 5bnl:

The structure of Deciphering the Mechanism of Carbonic Anhydrase Inhibition with Coumarins and Thiocoumarins also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the Deciphering the Mechanism of Carbonic Anhydrase Inhibition with Coumarins and Thiocoumarins (pdb code 5bnl). 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 Deciphering the Mechanism of Carbonic Anhydrase Inhibition with Coumarins and Thiocoumarins, PDB code: 5bnl:

Mercury binding site 1 out of 1 in 5bnl

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Mercury Binding Sites List in 5bnl

Mercury binding site 1 out of 1 in the Deciphering the Mechanism of Carbonic Anhydrase Inhibition with Coumarins and Thiocoumarins

Mono view

Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Deciphering the Mechanism of Carbonic Anhydrase Inhibition with Coumarins and Thiocoumarins within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Hg302 b:31.4 occ:1.00	O	A:GLN137	3.0	11.3	1.0
	O	A:HOH467	3.1	24.6	1.0
	CB	A:CYS206	3.2	9.8	1.0
	O	A:GLU205	3.2	8.5	1.0
	C	A:GLN137	3.3	10.9	1.0
	CA	A:CYS206	3.5	9.7	1.0
	C	A:GLU205	3.5	8.0	1.0
	O	A:VAL135	3.6	14.6	1.0
	N	A:CYS206	3.7	9.0	1.0
	N	A:GLN137	3.7	11.5	1.0
	N	A:PRO138	3.8	10.9	1.0
	C	A:GLN136	3.9	12.3	1.0
	O	A:HOH503	4.0	11.8	1.0
	CA	A:GLN137	4.0	11.7	1.0
	CA	A:PRO138	4.0	10.6	1.0
	C	A:VAL135	4.1	12.3	1.0
	N	A:GLU205	4.2	6.5	1.0
	O	A:GLN136	4.4	11.8	1.0
	CA	A:GLU205	4.4	8.1	1.0
	CA	A:GLN136	4.4	12.2	1.0
	N	A:GLN136	4.6	12.0	1.0
	SG	A:CYS206	4.6	16.2	1.0
	CB	A:LEU204	4.8	5.7	1.0
	C	A:LEU204	4.8	6.3	1.0
	CD	A:PRO138	4.8	11.2	1.0
	C	A:CYS206	4.9	8.6	1.0
	CA	A:VAL135	5.0	11.6	1.0

Reference:

A.Maresca, C.Temperini, L.Pochet, B.Masereel, A.Scozzafava, C.T.Supuran. Deciphering the Mechanism of Carbonic Anhydrase Inhibition with Coumarins and Thiocoumarins. J.Med.Chem. V. 53 335 2010.
ISSN: ISSN 0022-2623
PubMed: 19911821
DOI: 10.1021/JM901287J

Page generated: Sun Aug 11 05:39:48 2024

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