Manganese in PDB 1mr2: Structure of the Mt-Adprase in Complex with 1 MN2+ Ion and Amp-Cp (A Inhibitor), A Nudix Enzyme

Enzymatic activity of Structure of the Mt-Adprase in Complex with 1 MN2+ Ion and Amp-Cp (A Inhibitor), A Nudix Enzyme

All present enzymatic activity of Structure of the Mt-Adprase in Complex with 1 MN2+ Ion and Amp-Cp (A Inhibitor), A Nudix Enzyme:
3.6.1.13;

Protein crystallography data

The structure of Structure of the Mt-Adprase in Complex with 1 MN2+ Ion and Amp-Cp (A Inhibitor), A Nudix Enzyme, PDB code: 1mr2 was solved by L.-W.Kang, S.B.Gabelli, M.A.Bianchet, J.E.Cunningham, S.F.O'handley, L.M.Amzel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	30.00 / 2.30
*Space group*	P 6₁ 2 2
*Cell size a, b, c (Å), α, β, γ (°)*	63.894, 63.894, 182.059, 90.00, 90.00, 120.00
*R / R_free (%)*	20.5 / 26

Manganese Binding Sites:

The binding sites of Manganese atom in the Structure of the Mt-Adprase in Complex with 1 MN2+ Ion and Amp-Cp (A Inhibitor), A Nudix Enzyme (pdb code 1mr2). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Structure of the Mt-Adprase in Complex with 1 MN2+ Ion and Amp-Cp (A Inhibitor), A Nudix Enzyme, PDB code: 1mr2:

Manganese binding site 1 out of 1 in 1mr2

Go back to

Manganese Binding Sites List in 1mr2

Manganese binding site 1 out of 1 in the Structure of the Mt-Adprase in Complex with 1 MN2+ Ion and Amp-Cp (A Inhibitor), A Nudix Enzyme

Mono view

Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Structure of the Mt-Adprase in Complex with 1 MN2+ Ion and Amp-Cp (A Inhibitor), A Nudix Enzyme within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Mn401 b:56.8 occ:0.50	O3B	A:A12301	2.2	67.5	1.0
	O	A:ALA76	2.4	46.8	1.0
	O	A:HOH403	2.9	52.5	1.0
	PB	A:A12301	3.4	71.7	1.0
	C	A:ALA76	3.6	42.5	1.0
	O	A:HOH404	3.6	57.4	1.0
	O2A	A:A12301	3.7	79.4	1.0
	OE1	A:GLU97	3.7	72.2	1.0
	OE2	A:GLU93	3.8	53.9	1.0
	O2B	A:A12301	4.0	70.8	1.0
	O	A:HOH436	4.1	34.9	1.0
	C3A	A:A12301	4.2	74.7	1.0
	CD	A:GLU93	4.2	51.0	1.0
	OE1	A:GLN62	4.4	54.1	1.0
	N	A:ALA76	4.5	39.4	1.0
	PA	A:A12301	4.5	78.8	1.0
	CA	A:GLY77	4.5	41.2	1.0
	N	A:GLY77	4.5	41.0	1.0
	O	A:HOH405	4.5	37.0	1.0
	CA	A:ALA76	4.5	41.4	1.0
	O1B	A:A12301	4.6	72.9	1.0
	CD	A:GLU97	4.6	70.6	1.0
	CG	A:GLU93	4.7	49.6	1.0
	OE1	A:GLU93	4.8	50.2	1.0
	NE2	A:GLN62	4.9	55.1	1.0

Reference:

L.-W.Kang, S.B.Gabelli, J.E.Cunningham, S.F.O'handley, L.M.Amzel. Structure and Mechanism of Mt-Adprase, A Nudix Hydrolase From Mycobacterium Tuberculosis Structure V. 11 1015 2003.
ISSN: ISSN 0969-2126
PubMed: 12906832
DOI: 10.1016/S0969-2126(03)00154-0

Page generated: Sat Oct 5 11:44:41 2024

Last articles

Zn in 9J0N
Zn in 9J0O
Zn in 9J0P
Zn in 9FJX
Zn in 9EKB
Zn in 9C0F
Zn in 9CAH
Zn in 9CH0
Zn in 9CH3
Zn in 9CH1

	© Copyright 2008-2020 by atomistry.com
Home \| Site Map \| Copyright \| Contact us \| Privacy