Manganese in PDB 2j0b: Structure of the Catalytic Domain of Mouse Manic Fringe in Complex with Udp and Manganese

Enzymatic activity of Structure of the Catalytic Domain of Mouse Manic Fringe in Complex with Udp and Manganese

All present enzymatic activity of Structure of the Catalytic Domain of Mouse Manic Fringe in Complex with Udp and Manganese:
2.4.1.222;

Protein crystallography data

The structure of Structure of the Catalytic Domain of Mouse Manic Fringe in Complex with Udp and Manganese, PDB code: 2j0b was solved by M.Jinek, Y.-W.Chen, H.Clausen, S.M.Cohen, E.Conti, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	80.85 / 2.10
*Space group*	P 2₁ 2₁ 2
*Cell size a, b, c (Å), α, β, γ (°)*	161.760, 40.970, 38.370, 90.00, 90.00, 90.00
*R / R_free (%)*	17.7 / 22.1

Other elements in 2j0b:

The structure of Structure of the Catalytic Domain of Mouse Manic Fringe in Complex with Udp and Manganese also contains other interesting chemical elements:

Potassium

(K)

1 atom

Manganese Binding Sites:

The binding sites of Manganese atom in the Structure of the Catalytic Domain of Mouse Manic Fringe in Complex with Udp and Manganese (pdb code 2j0b). 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 Catalytic Domain of Mouse Manic Fringe in Complex with Udp and Manganese, PDB code: 2j0b:

Manganese binding site 1 out of 1 in 2j0b

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Manganese Binding Sites List in 2j0b

Manganese binding site 1 out of 1 in the Structure of the Catalytic Domain of Mouse Manic Fringe in Complex with Udp and Manganese

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 Catalytic Domain of Mouse Manic Fringe in Complex with Udp and Manganese within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Mn1321 b:34.0 occ:1.00	O1A	A:UDP1322	2.1	33.7	1.0
	OD2	A:ASP144	2.2	22.2	1.0
	O3B	A:UDP1322	2.3	38.9	1.0
	NE2	A:HIS256	2.3	22.9	1.0
	O	A:HOH2083	2.5	23.8	1.0
	O	A:HOH2084	2.5	13.7	1.0
	CG	A:ASP144	3.3	19.9	1.0
	CD2	A:HIS256	3.3	21.8	1.0
	CE1	A:HIS256	3.3	22.9	1.0
	PA	A:UDP1322	3.4	33.3	1.0
	PB	A:UDP1322	3.5	39.2	1.0
	OD1	A:ASP144	3.7	19.0	1.0
	O3A	A:UDP1322	3.8	39.9	1.0
	O	A:HOH2067	3.9	20.4	1.0
	O2B	A:UDP1322	4.1	42.7	1.0
	NH1	A:ARG70	4.2	23.1	1.0
	O	A:HOH2085	4.2	39.7	1.0
	O2A	A:UDP1322	4.3	32.6	1.0
	C5'	A:UDP1322	4.3	32.4	1.0
	O5'	A:UDP1322	4.3	33.0	1.0
	ND1	A:HIS256	4.4	22.1	1.0
	CG	A:HIS256	4.5	23.2	1.0
	CB	A:ASP144	4.5	18.0	1.0
	NH2	A:ARG70	4.5	24.9	1.0
	O	A:HOH2058	4.6	34.6	1.0
	O1B	A:UDP1322	4.6	41.1	1.0
	O	A:HOH2065	4.7	20.0	1.0
	O	A:TYR276	4.7	17.7	1.0
	CZ	A:ARG70	4.8	22.3	1.0
	O	A:HOH2068	4.8	37.9	1.0

Reference:

M.Jinek, Y.-W.Chen, H.Clausen, S.M.Cohen, E.Conti. Structural Insights Into the Notch-Modifying Glycosyltransferase Fringe Nat.Struct.Mol.Biol. V. 13 945 2006.
ISSN: ISSN 1545-9993
PubMed: 16964258
DOI: 10.1038/NSMB1144

Page generated: Sat Oct 5 14:30:30 2024

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