Mercury in PDB 1mua: Structure and Energetics of A Non-Proline Cis-Peptidyl Linkage in An Engineered Protein

Enzymatic activity of Structure and Energetics of A Non-Proline Cis-Peptidyl Linkage in An Engineered Protein

All present enzymatic activity of Structure and Energetics of A Non-Proline Cis-Peptidyl Linkage in An Engineered Protein:
4.2.1.1;

Protein crystallography data

The structure of Structure and Energetics of A Non-Proline Cis-Peptidyl Linkage in An Engineered Protein, PDB code: 1mua 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 / 1.70
*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 1mua:

The structure of Structure and Energetics of A Non-Proline Cis-Peptidyl Linkage in An Engineered Protein also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the Structure and Energetics of A Non-Proline Cis-Peptidyl Linkage in An Engineered Protein (pdb code 1mua). 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 Structure and Energetics of A Non-Proline Cis-Peptidyl Linkage in An Engineered Protein, PDB code: 1mua:

Mercury binding site 1 out of 1 in 1mua

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Mercury Binding Sites List in 1mua

Mercury binding site 1 out of 1 in the Structure and Energetics of A Non-Proline Cis-Peptidyl Linkage in An Engineered Protein

Mono view

Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Structure and Energetics of A Non-Proline Cis-Peptidyl Linkage in An Engineered Protein within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Hg331 b:15.4 occ:1.00	SG	A:CYS206	2.3	14.8	1.0
	O	A:GLN137	2.9	11.0	1.0
	CB	A:CYS206	3.1	11.0	1.0
	O	A:GLU205	3.3	8.9	1.0
	C	A:GLN137	3.4	11.4	1.0
	CA	A:CYS206	3.6	9.6	1.0
	C	A:GLU205	3.6	8.5	1.0
	N	A:GLN137	3.7	11.7	1.0
	O	A:VAL135	3.8	11.5	1.0
	N	A:CYS206	3.8	8.9	1.0
	C	A:GLN136	4.0	12.2	1.0
	N	A:PRO138	4.0	10.9	1.0
	CA	A:GLN137	4.1	11.7	1.0
	O	A:HOH308	4.1	23.8	1.0
	C	A:VAL135	4.1	11.7	1.0
	CA	A:PRO138	4.3	10.3	1.0
	N	A:GLN136	4.4	11.8	1.0
	CA	A:GLN136	4.4	12.5	1.0
	N	A:GLU205	4.4	7.4	1.0
	O	A:GLN136	4.5	12.0	1.0
	CA	A:GLU205	4.6	8.2	1.0
	O	A:HOH333	4.6	14.2	1.0
	CA	A:VAL135	4.9	11.7	1.0
	O	A:ALA134	5.0	11.8	1.0
	C	A:CYS206	5.0	8.8	1.0

Reference:

N.B.Tweedy, S.K.Nair, S.A.Paterno, C.A.Fierke, D.W.Christianson. Structure and Energetics of A Non-Proline Cis-Peptidyl Linkage in A Proline-202-->Alanine Carbonic Anhydrase II Variant. Biochemistry V. 32 10944 1993.
ISSN: ISSN 0006-2960
PubMed: 8218160
DOI: 10.1021/BI00092A003

Page generated: Fri Aug 8 09:15:54 2025

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