Magnesium in PDB 2oi7: E. Coli Glmu- Complex with Udp-Glcnac, Desulpho-Coa and Glcnac-1-PO4

Enzymatic activity of E. Coli Glmu- Complex with Udp-Glcnac, Desulpho-Coa and Glcnac-1-PO4

All present enzymatic activity of E. Coli Glmu- Complex with Udp-Glcnac, Desulpho-Coa and Glcnac-1-PO4:
2.3.1.157; 2.7.7.23;

Protein crystallography data

The structure of E. Coli Glmu- Complex with Udp-Glcnac, Desulpho-Coa and Glcnac-1-PO4, PDB code: 2oi7 was solved by L.R.Olsen, M.W.Vetting, S.L.Roderick, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	27.45 / 2.54
*Space group*	H 3 2
*Cell size a, b, c (Å), α, β, γ (°)*	102.969, 102.969, 644.076, 90.00, 90.00, 120.00
*R / R_free (%)*	20.9 / 24.7

Other elements in 2oi7:

The structure of E. Coli Glmu- Complex with Udp-Glcnac, Desulpho-Coa and Glcnac-1-PO4 also contains other interesting chemical elements:

Cobalt

(Co)

3 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the E. Coli Glmu- Complex with Udp-Glcnac, Desulpho-Coa and Glcnac-1-PO4 (pdb code 2oi7). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the E. Coli Glmu- Complex with Udp-Glcnac, Desulpho-Coa and Glcnac-1-PO4, PDB code: 2oi7:

Magnesium binding site 1 out of 1 in 2oi7

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Magnesium Binding Sites List in 2oi7

Magnesium binding site 1 out of 1 in the E. Coli Glmu- Complex with Udp-Glcnac, Desulpho-Coa and Glcnac-1-PO4

Mono view

Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of E. Coli Glmu- Complex with Udp-Glcnac, Desulpho-Coa and Glcnac-1-PO4 within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
B:Mg6000 b:26.1 occ:1.00	OD2	B:ASP105	2.0	20.3	1.0
	O	B:HOH8008	2.0	12.2	1.0
	O	B:HOH8064	2.1	17.6	1.0
	O2B	B:UD14001	2.2	14.7	1.0
	OD1	B:ASN227	2.3	17.2	1.0
	O2A	B:UD14001	2.3	17.4	1.0
	CG	B:ASP105	3.1	20.6	1.0
	CG	B:ASN227	3.3	15.8	1.0
	PA	B:UD14001	3.4	19.9	1.0
	PB	B:UD14001	3.4	16.5	1.0
	OD1	B:ASP105	3.5	20.2	1.0
	O3A	B:UD14001	3.5	16.6	1.0
	ND2	B:ASN227	3.6	14.2	1.0
	O6'	B:UD14001	3.7	21.1	1.0
	NZ	B:LYS25	3.7	24.1	1.0
	O	B:VAL226	4.1	19.8	1.0
	O5'	B:UD14001	4.2	19.9	1.0
	C5B	B:UD14001	4.2	21.8	1.0
	O5B	B:UD14001	4.2	19.7	1.0
	CB	B:ASP105	4.4	18.0	1.0
	O1B	B:UD14001	4.4	15.1	1.0
	O1'	B:UD14001	4.4	16.1	1.0
	C	B:VAL226	4.5	18.9	1.0
	O1A	B:UD14001	4.6	17.0	1.0
	CB	B:ASN227	4.6	17.3	1.0
	O	B:HOH8044	4.6	10.0	1.0
	N	B:VAL226	4.6	20.7	1.0
	C1'	B:UD14001	4.7	19.5	1.0
	C5'	B:UD14001	4.7	20.0	1.0
	C6'	B:UD14001	4.8	19.9	1.0
	CA	B:ASN227	4.9	19.6	1.0
	N	B:ASN227	4.9	19.4	1.0

Reference:

L.R.Olsen, M.W.Vetting, S.L.Roderick. Structure of the E. Coli Bifunctional Glmu Acetyltransferase Active Site with Substrates and Products. Protein Sci. V. 16 1230 2007.
ISSN: ISSN 0961-8368
PubMed: 17473010
DOI: 10.1110/PS.072779707

Page generated: Wed Aug 14 01:29:01 2024

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