Mercury in PDB 1heb: Structural Consequences of Hydrophilic Amino-Acid Substitutions in the Hydrophobic Pocket of Human Carbonic Anhydrase II

Enzymatic activity of Structural Consequences of Hydrophilic Amino-Acid Substitutions in the Hydrophobic Pocket of Human Carbonic Anhydrase II

All present enzymatic activity of Structural Consequences of Hydrophilic Amino-Acid Substitutions in the Hydrophobic Pocket of Human Carbonic Anhydrase II:
4.2.1.1;

Protein crystallography data

The structure of Structural Consequences of Hydrophilic Amino-Acid Substitutions in the Hydrophobic Pocket of Human Carbonic Anhydrase II, PDB code: 1heb 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)*	N/A / 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 (%)*	n/a / n/a

Other elements in 1heb:

The structure of Structural Consequences of Hydrophilic Amino-Acid Substitutions in the Hydrophobic Pocket 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 Consequences of Hydrophilic Amino-Acid Substitutions in the Hydrophobic Pocket of Human Carbonic Anhydrase II (pdb code 1heb). 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 Consequences of Hydrophilic Amino-Acid Substitutions in the Hydrophobic Pocket of Human Carbonic Anhydrase II, PDB code: 1heb:

Mercury binding site 1 out of 1 in 1heb

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Mercury Binding Sites List in 1heb

Mercury binding site 1 out of 1 in the Structural Consequences of Hydrophilic Amino-Acid Substitutions in the Hydrophobic Pocket 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 Consequences of Hydrophilic Amino-Acid Substitutions in the Hydrophobic Pocket of Human Carbonic Anhydrase II within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Hg263 b:17.3 occ:1.00	SG	A:CYS206	2.3	12.7	1.0
	O	A:GLN137	2.9	10.1	1.0
	CB	A:CYS206	3.2	10.1	1.0
	C	A:GLN137	3.4	10.4	1.0
	O	A:GLU205	3.5	8.1	1.0
	CA	A:CYS206	3.5	8.9	1.0
	N	A:GLN137	3.6	11.9	1.0
	O	A:VAL135	3.7	13.6	1.0
	N	A:CYS206	3.7	8.8	1.0
	C	A:GLU205	3.7	8.0	1.0
	C	A:GLN136	3.9	13.0	1.0
	CA	A:GLN137	4.0	11.0	1.0
	C	A:VAL135	4.0	13.5	1.0
	N	A:PRO138	4.0	9.6	1.0
	O	A:HOH300	4.1	12.1	1.0
	CA	A:GLN136	4.3	13.5	1.0
	N	A:GLN136	4.3	13.5	1.0
	CA	A:PRO138	4.4	9.4	1.0
	O	A:GLN136	4.4	12.8	1.0
	O	A:HOH318	4.5	8.7	1.0
	N	A:GLU205	4.6	7.1	1.0
	CA	A:GLU205	4.7	7.6	1.0
	CA	A:VAL135	4.8	13.5	1.0
	CB	A:LEU204	5.0	7.6	1.0
	C	A:CYS206	5.0	8.2	1.0

Reference:

S.K.Nair, D.W.Christianson. Structural Consequences of Hydrophilic Amino Acid Substitutions in the Hydrophobic Pocket of Human Carbonic Anhydrase II. Biochemistry V. 32 4506 1993.
ISSN: ISSN 0006-2960
PubMed: 8485129
DOI: 10.1021/BI00068A005

Page generated: Sat Aug 10 23:55:29 2024

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