Mercury in PDB 1i9p: Carbonic Anhydrase II (F131V) Complexed with 4-(Aminosulfonyl)-N-[(2, 4,6-Trifluorophenyl)Methyl]-Benzamide

Enzymatic activity of Carbonic Anhydrase II (F131V) Complexed with 4-(Aminosulfonyl)-N-[(2, 4,6-Trifluorophenyl)Methyl]-Benzamide

All present enzymatic activity of Carbonic Anhydrase II (F131V) Complexed with 4-(Aminosulfonyl)-N-[(2, 4,6-Trifluorophenyl)Methyl]-Benzamide:
4.2.1.1;

Protein crystallography data

The structure of Carbonic Anhydrase II (F131V) Complexed with 4-(Aminosulfonyl)-N-[(2, 4,6-Trifluorophenyl)Methyl]-Benzamide, PDB code: 1i9p was solved by C.-Y.Kim, P.P.Chandra, A.Jain, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	20.00 / 1.92
*Space group*	P 1 2₁ 1
*Cell size a, b, c (Å), α, β, γ (°)*	43.105, 42.111, 73.356, 90.00, 104.60, 90.00
*R / R_free (%)*	21.7 / 29

Other elements in 1i9p:

The structure of Carbonic Anhydrase II (F131V) Complexed with 4-(Aminosulfonyl)-N-[(2, 4,6-Trifluorophenyl)Methyl]-Benzamide also contains other interesting chemical elements:

Fluorine	(F)	3 atoms
Zinc	(Zn)	1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the Carbonic Anhydrase II (F131V) Complexed with 4-(Aminosulfonyl)-N-[(2, 4,6-Trifluorophenyl)Methyl]-Benzamide (pdb code 1i9p). 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 (F131V) Complexed with 4-(Aminosulfonyl)-N-[(2, 4,6-Trifluorophenyl)Methyl]-Benzamide, PDB code: 1i9p:

Mercury binding site 1 out of 1 in 1i9p

Go back to

Mercury Binding Sites List in 1i9p

Mercury binding site 1 out of 1 in the Carbonic Anhydrase II (F131V) Complexed with 4-(Aminosulfonyl)-N-[(2, 4,6-Trifluorophenyl)Methyl]-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 (F131V) Complexed with 4-(Aminosulfonyl)-N-[(2, 4,6-Trifluorophenyl)Methyl]-Benzamide within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Hg263 b:24.3 occ:1.00	SG	A:CYS206	1.5	2.1	1.0
	N	A:GLN137	2.7	20.6	1.0
	C	A:GLN136	2.9	21.9	1.0
	O	A:GLN137	2.9	20.2	1.0
	CB	A:CYS206	2.9	11.8	1.0
	O	A:VAL135	3.0	20.8	1.0
	C	A:GLN137	3.0	19.3	1.0
	CA	A:GLN137	3.3	21.1	1.0
	CA	A:GLN136	3.4	20.9	1.0
	C	A:VAL135	3.4	19.8	1.0
	O	A:GLN136	3.5	22.8	1.0
	N	A:GLN136	3.6	19.9	1.0
	N	A:PRO138	3.8	18.6	1.0
	CA	A:CYS206	4.1	12.6	1.0
	O	A:GLU205	4.4	14.6	1.0
	CA	A:PRO138	4.5	17.6	1.0
	CA	A:VAL135	4.5	19.2	1.0
	O	A:ALA134	4.5	17.1	1.0
	N	A:CYS206	4.6	13.1	1.0
	CB	A:GLN137	4.7	21.1	1.0
	C	A:GLU205	4.7	13.2	1.0
	CD	A:PRO138	4.8	17.7	1.0
	CB	A:GLN136	4.9	20.4	1.0
	O	A:HOH361	4.9	30.9	1.0

Reference:

C.Y.Kim, P.P.Chandra, A.Jain, D.W.Christianson. Fluoroaromatic-Fluoroaromatic Interactions Between Inhibitors Bound in the Crystal Lattice of Human Carbonic Anhydrase II. J.Am.Chem.Soc. V. 123 9620 2001.
ISSN: ISSN 0002-7863
PubMed: 11572683
DOI: 10.1021/JA011034P

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

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0

	© Copyright 2008-2020 by atomistry.com
Home \| Site Map \| Copyright \| Contact us \| Privacy