Mercury in PDB 1g4o: Carbonic Anhydrase II (F131V) Complexed with 4-(Aminosulfonyl)-N- Phenylmethylbenzamide

Enzymatic activity of Carbonic Anhydrase II (F131V) Complexed with 4-(Aminosulfonyl)-N- Phenylmethylbenzamide

All present enzymatic activity of Carbonic Anhydrase II (F131V) Complexed with 4-(Aminosulfonyl)-N- Phenylmethylbenzamide:
4.2.1.1;

Protein crystallography data

The structure of Carbonic Anhydrase II (F131V) Complexed with 4-(Aminosulfonyl)-N- Phenylmethylbenzamide, PDB code: 1g4o was solved by C.-Y.Kim, J.S.Chang, J.B.Doyon, T.T.Baird Jr., C.A.Fierke, 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 / 1.96
*Space group*	P 1 2₁ 1
*Cell size a, b, c (Å), α, β, γ (°)*	43.050, 42.230, 73.720, 90.00, 104.77, 90.00
*R / R_free (%)*	19.7 / 28.4

Other elements in 1g4o:

The structure of Carbonic Anhydrase II (F131V) Complexed with 4-(Aminosulfonyl)-N- Phenylmethylbenzamide also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the Carbonic Anhydrase II (F131V) Complexed with 4-(Aminosulfonyl)-N- Phenylmethylbenzamide (pdb code 1g4o). 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- Phenylmethylbenzamide, PDB code: 1g4o:

Mercury binding site 1 out of 1 in 1g4o

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Mercury Binding Sites List in 1g4o

Mercury binding site 1 out of 1 in the Carbonic Anhydrase II (F131V) Complexed with 4-(Aminosulfonyl)-N- Phenylmethylbenzamide

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- Phenylmethylbenzamide within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Hg263 b:8.4 occ:1.00	SG	A:CYS206	1.5	2.5	1.0
	N	A:GLN137	2.9	22.1	1.0
	CB	A:CYS206	3.0	14.5	1.0
	O	A:GLN137	3.0	18.0	1.0
	O	A:VAL135	3.1	24.0	1.0
	C	A:GLN136	3.1	23.8	1.0
	C	A:GLN137	3.2	19.8	1.0
	C	A:VAL135	3.5	22.0	1.0
	CA	A:GLN137	3.5	21.5	1.0
	CA	A:GLN136	3.5	23.8	1.0
	O	A:GLN136	3.6	22.4	1.0
	N	A:GLN136	3.7	21.2	1.0
	N	A:PRO138	4.0	17.2	1.0
	CA	A:CYS206	4.1	14.0	1.0
	O	A:GLU205	4.2	15.8	1.0
	O	A:HOH341	4.3	22.6	1.0
	CA	A:VAL135	4.5	19.9	1.0
	O	A:ALA134	4.5	21.9	1.0
	O	A:HOH345	4.6	61.1	1.0
	C	A:GLU205	4.6	11.6	1.0
	CA	A:PRO138	4.6	17.4	1.0
	N	A:CYS206	4.6	13.4	1.0
	CB	A:GLN137	4.9	19.0	1.0

Reference:

C.-Y.Kim, J.S.Chang, J.B.Doyon, T.T.Baird Jr., C.A.Fierke, A.Jain, D.W.Christianson. Contribution of Flourine to Protein-Ligand Affinity in the Binding of Flouroaromatic Inhibitors to Carbonic Anhydrase II J.Am.Chem.Soc. V. 122 12125 2000.
ISSN: ISSN 0002-7863
DOI: 10.1021/JA002627N

Page generated: Sat Aug 10 23:47:45 2024

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