Mercury in PDB 1cni: X-Ray Crystallographic Studies of Engineered Hydrogen Bond Networks in A Protein-Zinc Binding Site

Enzymatic activity of X-Ray Crystallographic Studies of Engineered Hydrogen Bond Networks in A Protein-Zinc Binding Site

All present enzymatic activity of X-Ray Crystallographic Studies of Engineered Hydrogen Bond Networks in A Protein-Zinc Binding Site:
4.2.1.1;

Protein crystallography data

The structure of X-Ray Crystallographic Studies of Engineered Hydrogen Bond Networks in A Protein-Zinc Binding Site, PDB code: 1cni was solved by C.A.Lesburg, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	8.00 / 1.80
*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 (%)*	16.1 / n/a

Other elements in 1cni:

The structure of X-Ray Crystallographic Studies of Engineered Hydrogen Bond Networks in A Protein-Zinc Binding Site also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the X-Ray Crystallographic Studies of Engineered Hydrogen Bond Networks in A Protein-Zinc Binding Site (pdb code 1cni). 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 X-Ray Crystallographic Studies of Engineered Hydrogen Bond Networks in A Protein-Zinc Binding Site, PDB code: 1cni:

Mercury binding site 1 out of 1 in 1cni

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Mercury Binding Sites List in 1cni

Mercury binding site 1 out of 1 in the X-Ray Crystallographic Studies of Engineered Hydrogen Bond Networks in A Protein-Zinc Binding Site

Mono view

Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of X-Ray Crystallographic Studies of Engineered Hydrogen Bond Networks in A Protein-Zinc Binding Site within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Hg262 b:19.6 occ:1.00	SG	A:CYS206	2.3	19.2	1.0
	O	A:GLN137	3.0	13.0	1.0
	CB	A:CYS206	3.1	12.7	1.0
	O	A:GLU205	3.4	7.7	1.0
	C	A:GLN137	3.4	13.6	1.0
	O	A:VAL135	3.5	14.9	1.0
	CA	A:CYS206	3.6	8.9	1.0
	C	A:GLU205	3.7	8.6	1.0
	N	A:GLN137	3.7	15.2	1.0
	N	A:CYS206	3.8	8.7	1.0
	C	A:GLN136	3.9	16.4	1.0
	C	A:VAL135	4.0	14.8	1.0
	N	A:PRO138	4.1	12.9	1.0
	CA	A:GLN137	4.1	13.9	1.0
	O	A:HOH318	4.2	22.8	1.0
	CA	A:GLN136	4.3	16.4	1.0
	CA	A:PRO138	4.3	11.4	1.0
	N	A:GLN136	4.4	15.0	1.0
	O	A:GLN136	4.4	16.4	1.0
	O	A:HOH325	4.4	17.0	1.0
	N	A:GLU205	4.5	8.6	1.0
	CA	A:GLU205	4.6	7.7	1.0
	O	A:HOH391	4.6	43.1	1.0
	CA	A:VAL135	4.8	14.4	1.0
	CB	A:LEU204	4.9	12.3	1.0
	O	A:ALA134	5.0	13.6	1.0

Reference:

C.A.Lesburg, D.W.Christianson. X-Ray Crystallographic Studies of Engineered Hydrogen Bond Networks in A Protein-Zinc Binding Site J.Am.Chem.Soc. V. 117 6838 1995.
ISSN: ISSN 0002-7863

Page generated: Sat Aug 10 23:24:01 2024

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