Mercury in PDB 5ca2: Conformational Mobility of His-64 in the Thr-200 (Right Arrow) Ser Mutant of Human Carbonic Anhydrase II

Enzymatic activity of Conformational Mobility of His-64 in the Thr-200 (Right Arrow) Ser Mutant of Human Carbonic Anhydrase II

All present enzymatic activity of Conformational Mobility of His-64 in the Thr-200 (Right Arrow) Ser Mutant of Human Carbonic Anhydrase II:
4.2.1.1;

Protein crystallography data

The structure of Conformational Mobility of His-64 in the Thr-200 (Right Arrow) Ser Mutant of Human Carbonic Anhydrase II, PDB code: 5ca2 was solved by R.S.Alexander, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	N/A / 2.10
*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 5ca2:

The structure of Conformational Mobility of His-64 in the Thr-200 (Right Arrow) Ser Mutant 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 Conformational Mobility of His-64 in the Thr-200 (Right Arrow) Ser Mutant of Human Carbonic Anhydrase II (pdb code 5ca2). 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 Conformational Mobility of His-64 in the Thr-200 (Right Arrow) Ser Mutant of Human Carbonic Anhydrase II, PDB code: 5ca2:

Mercury binding site 1 out of 1 in 5ca2

Go back to

Mercury Binding Sites List in 5ca2

Mercury binding site 1 out of 1 in the Conformational Mobility of His-64 in the Thr-200 (Right Arrow) Ser Mutant 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 Conformational Mobility of His-64 in the Thr-200 (Right Arrow) Ser Mutant of Human Carbonic Anhydrase II within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Hg263 b:16.2 occ:1.00	SG	A:CYS206	2.1	6.8	1.0
	O	A:GLN137	3.0	11.7	1.0
	CB	A:CYS206	3.2	6.4	1.0
	O	A:GLU205	3.3	6.4	1.0
	C	A:GLN137	3.4	11.9	1.0
	O	A:VAL135	3.5	13.3	1.0
	CA	A:CYS206	3.6	6.3	1.0
	C	A:GLU205	3.6	6.8	1.0
	N	A:CYS206	3.7	6.4	1.0
	N	A:GLN137	3.7	12.7	1.0
	O	A:HOH312	3.9	9.0	1.0
	C	A:GLN136	4.0	13.2	1.0
	N	A:PRO138	4.0	11.4	1.0
	CA	A:GLN137	4.0	12.5	1.0
	C	A:VAL135	4.1	13.1	1.0
	CA	A:PRO138	4.3	11.0	1.0
	N	A:GLU205	4.4	7.4	1.0
	O	A:HOH337	4.4	11.5	1.0
	CA	A:GLN136	4.4	13.4	1.0
	O	A:GLN136	4.4	12.9	1.0
	N	A:GLN136	4.5	13.3	1.0
	CA	A:GLU205	4.6	7.0	1.0
	CB	A:LEU204	4.8	7.9	1.0
	O	A:ALA134	4.9	13.1	1.0
	CA	A:VAL135	4.9	12.9	1.0
	C	A:CYS206	4.9	5.8	1.0
	C	A:LEU204	5.0	7.6	1.0

Reference:

J.F.Krebs, C.A.Fierke, R.S.Alexander, D.W.Christianson. Conformational Mobility of His-64 in the Thr-200----Ser Mutant of Human Carbonic Anhydrase II. Biochemistry V. 30 9153 1991.
ISSN: ISSN 0006-2960
PubMed: 1909891
DOI: 10.1021/BI00102A005

Page generated: Sun Aug 11 06:12:12 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