Manganese in PDB 1i08: Crystal Structure Analysis of the H30A Mutant of Manganese Superoxide Dismutase From E. Coli

Enzymatic activity of Crystal Structure Analysis of the H30A Mutant of Manganese Superoxide Dismutase From E. Coli

All present enzymatic activity of Crystal Structure Analysis of the H30A Mutant of Manganese Superoxide Dismutase From E. Coli:
1.15.1.1;

Protein crystallography data

The structure of Crystal Structure Analysis of the H30A Mutant of Manganese Superoxide Dismutase From E. Coli, PDB code: 1i08 was solved by R.A.Edwards, M.M.Whittaker, J.W.Whittaker, E.N.Baker, G.B.Jameson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	40.00 / 2.20
*Space group*	C 2 2 2₁
*Cell size a, b, c (Å), α, β, γ (°)*	100.681, 109.110, 181.072, 90.00, 90.00, 90.00
*R / R_free (%)*	18.4 / 21.1

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure Analysis of the H30A Mutant of Manganese Superoxide Dismutase From E. Coli (pdb code 1i08). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the Crystal Structure Analysis of the H30A Mutant of Manganese Superoxide Dismutase From E. Coli, PDB code: 1i08:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in 1i08

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Manganese Binding Sites List in 1i08

Manganese binding site 1 out of 4 in the Crystal Structure Analysis of the H30A Mutant of Manganese Superoxide Dismutase From E. Coli

Mono view

Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure Analysis of the H30A Mutant of Manganese Superoxide Dismutase From E. Coli within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Mn206 b:14.0 occ:1.00	OD2	A:ASP167	1.9	11.4	1.0
	NE2	A:HIS171	2.1	13.6	1.0
	NE2	A:HIS26	2.2	16.5	1.0
	NE2	A:HIS81	2.2	14.3	1.0
	O	A:HOH278	2.3	6.5	1.0
	CE1	A:HIS26	3.0	14.8	1.0
	CE1	A:HIS171	3.1	14.2	1.0
	CG	A:ASP167	3.1	14.5	1.0
	CE1	A:HIS81	3.2	13.1	1.0
	CD2	A:HIS171	3.2	14.0	1.0
	CD2	A:HIS81	3.2	13.9	1.0
	CD2	A:HIS26	3.2	16.0	1.0
	OD1	A:ASP167	3.6	13.9	1.0
	ND1	A:HIS26	4.2	15.8	1.0
	ND1	A:HIS171	4.2	11.5	1.0
	ND1	A:HIS81	4.3	12.9	1.0
	CG	A:HIS171	4.3	13.5	1.0
	CB	A:ASP167	4.3	11.8	1.0
	CG	A:HIS26	4.3	16.1	1.0
	CG	A:HIS81	4.3	13.7	1.0
	CZ2	A:TRP128	4.6	10.9	1.0
	CB	A:TRP169	4.6	11.2	1.0
	NE2	A:GLN146	4.8	10.9	1.0
	CG	A:TRP169	4.8	12.3	1.0
	CB	A:ALA172	4.8	11.6	1.0

Manganese binding site 2 out of 4 in 1i08

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Manganese Binding Sites List in 1i08

Manganese binding site 2 out of 4 in the Crystal Structure Analysis of the H30A Mutant of Manganese Superoxide Dismutase From E. Coli

Mono view

Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure Analysis of the H30A Mutant of Manganese Superoxide Dismutase From E. Coli within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
B:Mn206 b:15.5 occ:1.00	OD2	B:ASP167	2.0	16.2	1.0
	NE2	B:HIS26	2.2	16.3	1.0
	NE2	B:HIS81	2.2	17.1	1.0
	NE2	B:HIS171	2.2	16.8	1.0
	O	B:HOH7963	2.2	10.4	1.0
	CE1	B:HIS26	3.0	17.1	1.0
	CG	B:ASP167	3.1	19.3	1.0
	CE1	B:HIS171	3.1	17.4	1.0
	CE1	B:HIS81	3.2	16.3	1.0
	CD2	B:HIS81	3.2	16.7	1.0
	CD2	B:HIS26	3.2	16.9	1.0
	CD2	B:HIS171	3.3	15.9	1.0
	OD1	B:ASP167	3.6	18.5	1.0
	ND1	B:HIS26	4.1	14.9	1.0
	ND1	B:HIS81	4.3	16.4	1.0
	CG	B:HIS26	4.3	16.0	1.0
	ND1	B:HIS171	4.3	15.8	1.0
	CB	B:ASP167	4.3	14.9	1.0
	CG	B:HIS81	4.3	17.1	1.0
	CG	B:HIS171	4.4	14.0	1.0
	CZ2	B:TRP128	4.5	16.4	1.0
	CB	B:TRP169	4.6	11.2	1.0
	NE2	B:GLN146	4.7	14.4	1.0
	CG	B:TRP169	4.8	9.1	1.0
	CB	B:ALA172	4.9	11.6	1.0

Manganese binding site 3 out of 4 in 1i08

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Manganese Binding Sites List in 1i08

Manganese binding site 3 out of 4 in the Crystal Structure Analysis of the H30A Mutant of Manganese Superoxide Dismutase From E. Coli

Mono view

Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Crystal Structure Analysis of the H30A Mutant of Manganese Superoxide Dismutase From E. Coli within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
C:Mn206 b:14.4 occ:1.00	OD2	C:ASP167	1.9	15.1	1.0
	NE2	C:HIS81	2.2	14.4	1.0
	NE2	C:HIS26	2.2	11.4	1.0
	NE2	C:HIS171	2.2	15.1	1.0
	O	C:HOH7964	2.3	11.3	1.0
	CG	C:ASP167	3.0	17.5	1.0
	CE1	C:HIS81	3.1	15.9	1.0
	CE1	C:HIS26	3.1	11.0	1.0
	CE1	C:HIS171	3.2	11.9	1.0
	CD2	C:HIS81	3.2	14.9	1.0
	CD2	C:HIS171	3.3	16.5	1.0
	CD2	C:HIS26	3.3	10.8	1.0
	OD1	C:ASP167	3.5	17.2	1.0
	ND1	C:HIS81	4.2	14.2	1.0
	ND1	C:HIS26	4.3	12.6	1.0
	CB	C:ASP167	4.3	14.1	1.0
	CG	C:HIS81	4.3	15.2	1.0
	ND1	C:HIS171	4.3	12.4	1.0
	CG	C:HIS26	4.4	12.9	1.0
	CG	C:HIS171	4.4	14.2	1.0
	CZ2	C:TRP128	4.5	15.5	1.0
	CB	C:TRP169	4.6	12.1	1.0
	NE2	C:GLN146	4.7	15.3	1.0
	CG	C:TRP169	4.8	13.5	1.0
	CB	C:ALA172	4.8	14.0	1.0
	CH2	C:TRP128	4.9	16.8	1.0

Manganese binding site 4 out of 4 in 1i08

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Manganese Binding Sites List in 1i08

Manganese binding site 4 out of 4 in the Crystal Structure Analysis of the H30A Mutant of Manganese Superoxide Dismutase From E. Coli

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Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Crystal Structure Analysis of the H30A Mutant of Manganese Superoxide Dismutase From E. Coli within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
D:Mn206 b:13.9 occ:1.00	OD2	D:ASP167	2.0	12.8	1.0
	NE2	D:HIS81	2.1	12.2	1.0
	NE2	D:HIS26	2.1	12.1	1.0
	NE2	D:HIS171	2.2	14.2	1.0
	O	D:HOH7965	2.2	15.4	1.0
	CE1	D:HIS26	3.0	13.1	1.0
	CE1	D:HIS81	3.1	13.1	1.0
	CG	D:ASP167	3.1	13.1	1.0
	CE1	D:HIS171	3.1	13.9	1.0
	CD2	D:HIS81	3.2	12.2	1.0
	CD2	D:HIS26	3.2	12.9	1.0
	CD2	D:HIS171	3.3	10.8	1.0
	OD1	D:ASP167	3.5	11.5	1.0
	ND1	D:HIS26	4.2	14.2	1.0
	ND1	D:HIS81	4.2	11.8	1.0
	ND1	D:HIS171	4.3	13.0	1.0
	CG	D:HIS81	4.3	12.8	1.0
	CG	D:HIS26	4.3	13.5	1.0
	CB	D:ASP167	4.3	10.8	1.0
	CG	D:HIS171	4.4	13.9	1.0
	CZ2	D:TRP128	4.5	14.1	1.0
	CB	D:TRP169	4.6	13.7	1.0
	NE2	D:GLN146	4.7	13.6	1.0
	CG	D:TRP169	4.8	12.9	1.0
	CB	D:ALA172	4.9	11.4	1.0
	CH2	D:TRP128	5.0	15.4	1.0

Reference:

R.A.Edwards, M.M.Whittaker, J.W.Whittaker, E.N.Baker, G.B.Jameson. Removing A Hydrogen Bond in the Dimer Interface of Escherichia Coli Manganese Superoxide Dismutase Alters Structure and Reactivity. Biochemistry V. 40 4622 2001.
ISSN: ISSN 0006-2960
PubMed: 11294629
DOI: 10.1021/BI002403H

Page generated: Tue Dec 15 03:49:10 2020

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