Mercury in PDB 1yda: Structural Basis of Inhibitor Affinity to Variants of Human Carbonic Anhydrase II

Enzymatic activity of Structural Basis of Inhibitor Affinity to Variants of Human Carbonic Anhydrase II

All present enzymatic activity of Structural Basis of Inhibitor Affinity to Variants of Human Carbonic Anhydrase II:
4.2.1.1;

Protein crystallography data

The structure of Structural Basis of Inhibitor Affinity to Variants of Human Carbonic Anhydrase II, PDB code: 1yda was solved by S.K.Nair, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	6.50 / 2.10
*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 (%)*	n/a / n/a

Other elements in 1yda:

The structure of Structural Basis of Inhibitor Affinity to Variants of Human Carbonic Anhydrase II also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the Structural Basis of Inhibitor Affinity to Variants of Human Carbonic Anhydrase II (pdb code 1yda). 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 Structural Basis of Inhibitor Affinity to Variants of Human Carbonic Anhydrase II, PDB code: 1yda:

Mercury binding site 1 out of 1 in 1yda

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Mercury Binding Sites List in 1yda

Mercury binding site 1 out of 1 in the Structural Basis of Inhibitor Affinity to Variants of Human Carbonic Anhydrase II

Mono view

Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Structural Basis of Inhibitor Affinity to Variants of Human Carbonic Anhydrase II within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Hg263 b:16.4 occ:1.00	SG	A:CYS206	2.1	7.6	1.0
	O	A:GLN137	2.8	6.4	1.0
	CB	A:CYS206	3.1	9.4	1.0
	O	A:GLU205	3.1	2.6	1.0
	C	A:GLN137	3.2	7.4	1.0
	N	A:GLN137	3.3	10.5	1.0
	O	A:VAL135	3.4	7.9	1.0
	C	A:GLU205	3.7	7.3	1.0
	CA	A:CYS206	3.7	6.9	1.0
	CA	A:GLN137	3.8	8.9	1.0
	C	A:GLN136	3.9	11.1	1.0
	N	A:PRO138	3.9	5.7	1.0
	C	A:VAL135	3.9	8.4	1.0
	N	A:CYS206	4.1	5.2	1.0
	O	A:HOH294	4.2	13.0	1.0
	CA	A:PRO138	4.3	5.4	1.0
	O	A:HOH306	4.4	19.2	1.0
	CA	A:GLN136	4.4	9.9	1.0
	N	A:GLN136	4.5	7.8	1.0
	O	A:GLN136	4.5	11.8	1.0
	CA	A:VAL135	4.6	7.9	1.0
	N	A:GLU205	4.7	8.6	1.0
	CA	A:GLU205	4.8	5.8	1.0
	CD	A:PRO138	4.8	6.6	1.0
	O	A:ALA134	4.9	11.1	1.0

Reference:

S.K.Nair, J.F.Krebs, D.W.Christianson, C.A.Fierke. Structural Basis of Inhibitor Affinity to Variants of Human Carbonic Anhydrase II. Biochemistry V. 34 3981 1995.
ISSN: ISSN 0006-2960
PubMed: 7696263
DOI: 10.1021/BI00012A016

Page generated: Fri Aug 8 09:38:53 2025

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