Mercury in PDB 1sdn: Crystal Structure of A Deacylation-Defective Mutant of Penicillin-Binding Protein 5 Modified By Mercury

Enzymatic activity of Crystal Structure of A Deacylation-Defective Mutant of Penicillin-Binding Protein 5 Modified By Mercury

All present enzymatic activity of Crystal Structure of A Deacylation-Defective Mutant of Penicillin-Binding Protein 5 Modified By Mercury:
3.4.16.4;

Protein crystallography data

The structure of Crystal Structure of A Deacylation-Defective Mutant of Penicillin-Binding Protein 5 Modified By Mercury, PDB code: 1sdn was solved by G.Nicola, R.A.Nicholas, C.Davies, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	15.00 / 2.50
*Space group*	P 3₂
*Cell size a, b, c (Å), α, β, γ (°)*	50.700, 50.700, 140.300, 90.00, 90.00, 120.00
*R / R_free (%)*	17.1 / 24.1

Mercury Binding Sites:

The binding sites of Mercury atom in the Crystal Structure of A Deacylation-Defective Mutant of Penicillin-Binding Protein 5 Modified By Mercury (pdb code 1sdn). 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 Crystal Structure of A Deacylation-Defective Mutant of Penicillin-Binding Protein 5 Modified By Mercury, PDB code: 1sdn:

Mercury binding site 1 out of 1 in 1sdn

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Mercury Binding Sites List in 1sdn

Mercury binding site 1 out of 1 in the Crystal Structure of A Deacylation-Defective Mutant of Penicillin-Binding Protein 5 Modified By Mercury

Mono view

Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Crystal Structure of A Deacylation-Defective Mutant of Penicillin-Binding Protein 5 Modified By Mercury within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Hg401 b:31.3 occ:1.00	SG	A:CYS115	2.5	27.8	1.0
	OD2	A:ASP105	2.7	24.9	1.0
	OD1	A:ASP105	2.8	23.3	1.0
	CG	A:ASP105	3.2	26.3	1.0
	CB	A:CYS115	3.4	25.7	1.0
	CA	A:CYS115	3.6	25.7	1.0
	CG2	A:THR50	3.7	15.1	1.0
	CD	A:LYS47	4.0	20.4	1.0
	CB	A:THR50	4.2	16.2	1.0
	CG	A:LYS47	4.3	18.5	1.0
	NZ	A:LYS47	4.5	22.9	1.0
	C	A:CYS115	4.5	25.5	1.0
	O	A:CYS115	4.6	26.0	1.0
	CB	A:LYS47	4.6	17.4	1.0
	N	A:CYS115	4.6	25.5	1.0
	CB	A:ASP105	4.7	27.6	1.0
	CE	A:LYS47	4.7	21.5	1.0
	O	A:VAL150	4.8	20.9	1.0
	OG1	A:THR50	4.8	14.8	1.0
	CD1	A:ILE54	4.8	23.9	1.0

Reference:

G.Nicola, A.Fedarovich, R.A.Nicholas, C.Davies. A Large Displacement of the Sxn Motif of CYS115-Modified Penicillin-Binding Protein 5 From Escherichia Coli. Biochem.J. V. 392 55 2005.
ISSN: ISSN 0264-6021
PubMed: 16038617
DOI: 10.1042/BJ20050449

Page generated: Sun Aug 11 01:39:34 2024

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