Mercury in PDB 4mlx: Structure of A Bidentate 3-Hydroxy-4H-Pyran-4-Thione Ligand Bound to Hcaii

Enzymatic activity of Structure of A Bidentate 3-Hydroxy-4H-Pyran-4-Thione Ligand Bound to Hcaii

All present enzymatic activity of Structure of A Bidentate 3-Hydroxy-4H-Pyran-4-Thione Ligand Bound to Hcaii:
4.2.1.1;

Protein crystallography data

The structure of Structure of A Bidentate 3-Hydroxy-4H-Pyran-4-Thione Ligand Bound to Hcaii, PDB code: 4mlx was solved by D.P.Martin, S.M.Cohen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	25.33 / 1.65
*Space group*	P 1 2₁ 1
*Cell size a, b, c (Å), α, β, γ (°)*	42.117, 41.389, 71.823, 90.00, 104.03, 90.00
*R / R_free (%)*	15.7 / 20

Other elements in 4mlx:

The structure of Structure of A Bidentate 3-Hydroxy-4H-Pyran-4-Thione Ligand Bound to Hcaii also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the Structure of A Bidentate 3-Hydroxy-4H-Pyran-4-Thione Ligand Bound to Hcaii (pdb code 4mlx). 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 of A Bidentate 3-Hydroxy-4H-Pyran-4-Thione Ligand Bound to Hcaii, PDB code: 4mlx:

Mercury binding site 1 out of 1 in 4mlx

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Mercury Binding Sites List in 4mlx

Mercury binding site 1 out of 1 in the Structure of A Bidentate 3-Hydroxy-4H-Pyran-4-Thione Ligand Bound to Hcaii

Mono view

Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Structure of A Bidentate 3-Hydroxy-4H-Pyran-4-Thione Ligand Bound to Hcaii within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Hg302 b:16.8 occ:1.00	HG	A:MBO302	0.0	16.8	1.0
	CE1	A:MBO302	2.2	15.3	1.0
	SG	A:CYS206	2.3	8.9	1.0
	O	A:VAL135	2.9	11.0	1.0
	CE2	A:MBO302	3.0	17.4	1.0
	O	A:GLN137	3.1	5.8	1.0
	CE6	A:MBO302	3.2	15.9	1.0
	CB	A:CYS206	3.3	6.1	1.0
	CA	A:CYS206	3.5	3.6	1.0
	N	A:GLN137	3.5	7.2	1.0
	C	A:GLN137	3.6	5.7	1.0
	O	A:GLU205	3.7	6.4	1.0
	N	A:CYS206	3.7	5.3	1.0
	C	A:GLU205	3.7	5.6	1.0
	C	A:VAL135	3.7	8.4	1.0
	N	A:GLU205	4.0	6.8	1.0
	O	A:HOH479	4.0	19.4	1.0
	C	A:GLN136	4.0	9.7	1.0
	CB	A:LEU204	4.1	6.1	1.0
	CA	A:GLN137	4.2	6.9	1.0
	CE3	A:MBO302	4.3	14.8	1.0
	N	A:GLN136	4.3	9.1	1.0
	N	A:PRO138	4.4	8.7	1.0
	CA	A:GLN136	4.4	9.3	1.0
	CA	A:VAL135	4.4	7.8	1.0
	C	A:LEU204	4.4	5.3	1.0
	CA	A:GLU205	4.4	5.2	1.0
	CE5	A:MBO302	4.5	18.4	1.0
	CA	A:PRO138	4.6	8.2	1.0
	O	A:ALA134	4.7	9.0	1.0
	O	A:GLN136	4.8	8.9	1.0
	CA	A:LEU204	4.8	6.1	1.0
	CE4	A:MBO302	4.8	19.0	1.0
	C	A:CYS206	5.0	3.8	1.0
	O	A:LEU204	5.0	5.7	1.0

Reference:

D.P.Martin, P.G.Blachly, A.R.Marts, T.M.Woodruff, C.A.De Oliveira, J.A.Mccammon, D.L.Tierney, S.M.Cohen. 'Unconventional' Coordination Chemistry By Metal Chelating Fragments in A Metalloprotein Active Site. J.Am.Chem.Soc. V. 136 5400 2014.
ISSN: ISSN 0002-7863
PubMed: 24635441
DOI: 10.1021/JA500616M

Page generated: Fri Aug 8 10:33:09 2025

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