Mercury in PDB 1okm: Carbonic Anhydrase II Complex with the 1OKM Inhibitor 4- Sulfonamide-[1-(4-Aminobutane)]Benzamide

Enzymatic activity of Carbonic Anhydrase II Complex with the 1OKM Inhibitor 4- Sulfonamide-[1-(4-Aminobutane)]Benzamide

All present enzymatic activity of Carbonic Anhydrase II Complex with the 1OKM Inhibitor 4- Sulfonamide-[1-(4-Aminobutane)]Benzamide:
4.2.1.1;

Protein crystallography data

The structure of Carbonic Anhydrase II Complex with the 1OKM Inhibitor 4- Sulfonamide-[1-(4-Aminobutane)]Benzamide, PDB code: 1okm was solved by D.Elbaum, S.K.Nair, M.W.Patchan, R.B.Thompson, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	N/A / 2.20
*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 (%)*	16.2 / 21.7

Other elements in 1okm:

The structure of Carbonic Anhydrase II Complex with the 1OKM Inhibitor 4- Sulfonamide-[1-(4-Aminobutane)]Benzamide also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the Carbonic Anhydrase II Complex with the 1OKM Inhibitor 4- Sulfonamide-[1-(4-Aminobutane)]Benzamide (pdb code 1okm). 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 Complex with the 1OKM Inhibitor 4- Sulfonamide-[1-(4-Aminobutane)]Benzamide, PDB code: 1okm:

Mercury binding site 1 out of 1 in 1okm

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Mercury Binding Sites List in 1okm

Mercury binding site 1 out of 1 in the Carbonic Anhydrase II Complex with the 1OKM Inhibitor 4- Sulfonamide-[1-(4-Aminobutane)]Benzamide

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 Complex with the 1OKM Inhibitor 4- Sulfonamide-[1-(4-Aminobutane)]Benzamide within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Hg531 b:19.8 occ:1.00	SG	A:CYS206	2.0	11.2	1.0
	O	A:HOH400	2.2	31.5	1.0
	CB	A:CYS206	3.0	10.3	1.0
	O	A:GLN137	3.1	7.5	1.0
	O	A:GLU205	3.4	6.8	1.0
	CA	A:CYS206	3.4	8.5	1.0
	C	A:GLN137	3.4	8.8	1.0
	C	A:GLU205	3.6	8.0	1.0
	N	A:GLN137	3.6	12.0	1.0
	N	A:CYS206	3.6	7.7	1.0
	O	A:VAL135	3.8	14.0	1.0
	C	A:GLN136	3.8	14.1	1.0
	O	A:HOH304	3.9	9.1	1.0
	O	A:HOH376	3.9	33.4	1.0
	N	A:PRO138	4.1	7.7	1.0
	CA	A:GLN137	4.1	11.1	1.0
	C	A:VAL135	4.1	12.5	1.0
	CA	A:GLN136	4.2	14.9	1.0
	N	A:GLN136	4.3	13.6	1.0
	O	A:GLN136	4.3	15.0	1.0
	N	A:GLU205	4.3	6.6	1.0
	CA	A:PRO138	4.4	8.0	1.0
	O	A:HOH325	4.5	15.1	1.0
	CA	A:GLU205	4.6	6.9	1.0
	CB	A:LEU204	4.7	5.8	1.0
	C	A:LEU204	4.9	6.7	1.0
	C	A:CYS206	4.9	8.7	1.0
	CA	A:VAL135	5.0	14.4	1.0
	O	A:ALA134	5.0	13.0	1.0

Reference:

D.Elbaum, S.K.Nair, M.W.Patchan, R.B.Thompson, D.W.Christianson. Structure-Based Design of A Sulfonamide Probe For Fluorescence Anisotropy Detection of Zinc with A Carbonic Anhydrase-Based Biosensor. J.Am.Chem.Soc. V. 118 8381 1996.
ISSN: ISSN 0002-7863

Page generated: Sun Aug 11 01:00:59 2024

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