Mercury in PDB 1ugf: Human Carbonic Anhydrase II [Hcaii] (E.C.4.2.1.1) Mutant with Ala 65 Replaced By Thr (A65T)

Enzymatic activity of Human Carbonic Anhydrase II [Hcaii] (E.C.4.2.1.1) Mutant with Ala 65 Replaced By Thr (A65T)

All present enzymatic activity of Human Carbonic Anhydrase II [Hcaii] (E.C.4.2.1.1) Mutant with Ala 65 Replaced By Thr (A65T):
4.2.1.1;

Protein crystallography data

The structure of Human Carbonic Anhydrase II [Hcaii] (E.C.4.2.1.1) Mutant with Ala 65 Replaced By Thr (A65T), PDB code: 1ugf was solved by L.R.Scolnick, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	6.50 / 2.00
*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 (%)*	17.3 / 23.2

Other elements in 1ugf:

The structure of Human Carbonic Anhydrase II [Hcaii] (E.C.4.2.1.1) Mutant with Ala 65 Replaced By Thr (A65T) also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the Human Carbonic Anhydrase II [Hcaii] (E.C.4.2.1.1) Mutant with Ala 65 Replaced By Thr (A65T) (pdb code 1ugf). 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 Human Carbonic Anhydrase II [Hcaii] (E.C.4.2.1.1) Mutant with Ala 65 Replaced By Thr (A65T), PDB code: 1ugf:

Mercury binding site 1 out of 1 in 1ugf

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Mercury Binding Sites List in 1ugf

Mercury binding site 1 out of 1 in the Human Carbonic Anhydrase II [Hcaii] (E.C.4.2.1.1) Mutant with Ala 65 Replaced By Thr (A65T)

Mono view

Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Human Carbonic Anhydrase II [Hcaii] (E.C.4.2.1.1) Mutant with Ala 65 Replaced By Thr (A65T) within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Hg483 b:24.5 occ:1.00	SG	A:CYS206	2.3	21.5	1.0
	O	A:GLN137	3.0	13.7	1.0
	CB	A:CYS206	3.1	15.1	1.0
	O	A:GLU205	3.3	12.8	1.0
	C	A:GLN137	3.4	15.9	1.0
	CA	A:CYS206	3.5	12.9	1.0
	N	A:GLN137	3.6	16.6	1.0
	C	A:GLU205	3.6	12.5	1.0
	O	A:VAL135	3.7	19.0	1.0
	N	A:CYS206	3.7	11.3	1.0
	O	A:HOH331	3.8	19.9	1.0
	C	A:GLN136	3.9	18.3	1.0
	N	A:PRO138	4.0	14.4	1.0
	CA	A:GLN137	4.0	15.2	1.0
	C	A:VAL135	4.1	17.3	1.0
	CA	A:GLN136	4.2	18.6	1.0
	CA	A:PRO138	4.3	15.6	1.0
	N	A:GLN136	4.3	17.3	1.0
	O	A:GLN136	4.4	18.3	1.0
	N	A:GLU205	4.5	13.2	1.0
	O	A:HOH365	4.5	16.8	1.0
	CA	A:GLU205	4.6	11.6	1.0
	CA	A:VAL135	4.9	17.8	1.0
	CB	A:LEU204	4.9	19.4	1.0
	O	A:ALA134	5.0	19.2	1.0

Reference:

L.R.Scolnick, D.W.Christianson. X-Ray Crystallographic Studies of Alanine-65 Variants of Carbonic Anhydrase II Reveal the Structural Basis of Compromised Proton Transfer in Catalysis. Biochemistry V. 35 16429 1996.
ISSN: ISSN 0006-2960
PubMed: 8987974
DOI: 10.1021/BI9617872

Page generated: Sun Aug 11 01:41:04 2024

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