Magnesium in PDB 2yqh: Crystal Structure of Uridine-Diphospho-N-Acetylglucosamine Pyrophosphorylase From Candida Albicans, in the Substrate-Binding Form

Enzymatic activity of Crystal Structure of Uridine-Diphospho-N-Acetylglucosamine Pyrophosphorylase From Candida Albicans, in the Substrate-Binding Form

All present enzymatic activity of Crystal Structure of Uridine-Diphospho-N-Acetylglucosamine Pyrophosphorylase From Candida Albicans, in the Substrate-Binding Form:
2.7.7.23;

Protein crystallography data

The structure of Crystal Structure of Uridine-Diphospho-N-Acetylglucosamine Pyrophosphorylase From Candida Albicans, in the Substrate-Binding Form, PDB code: 2yqh was solved by K.Miki, D.Maruyama, Y.Nishitani, T.Nonaka, A.Kita, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	38.31 / 2.30
*Space group*	P 1
*Cell size a, b, c (Å), α, β, γ (°)*	47.431, 61.804, 90.438, 90.01, 97.72, 92.88
*R / R_free (%)*	19.3 / 23.8

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Uridine-Diphospho-N-Acetylglucosamine Pyrophosphorylase From Candida Albicans, in the Substrate-Binding Form (pdb code 2yqh). 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 Crystal Structure of Uridine-Diphospho-N-Acetylglucosamine Pyrophosphorylase From Candida Albicans, in the Substrate-Binding Form, PDB code: 2yqh:

Magnesium binding site 1 out of 1 in 2yqh

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Magnesium Binding Sites List in 2yqh

Magnesium binding site 1 out of 1 in the Crystal Structure of Uridine-Diphospho-N-Acetylglucosamine Pyrophosphorylase From Candida Albicans, in the Substrate-Binding Form

Mono view

Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Uridine-Diphospho-N-Acetylglucosamine Pyrophosphorylase From Candida Albicans, in the Substrate-Binding Form within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Mg1201 b:28.1 occ:0.70	OG1	A:THR77	2.2	22.6	1.0
	O	A:ASN74	2.3	29.7	1.0
	O	A:THR77	2.4	21.2	1.0
	O	A:HOH1447	2.7	26.8	1.0
	OD1	A:ASN74	2.7	38.4	1.0
	C	A:THR77	2.9	21.1	1.0
	CB	A:THR77	3.3	21.5	1.0
	C	A:ASN74	3.3	30.3	1.0
	CA	A:THR77	3.4	22.6	1.0
	CG	A:ASN74	3.4	37.8	1.0
	N	A:THR77	3.6	23.5	1.0
	CA	A:ASN74	3.8	32.4	1.0
	N	A:ALA78	3.8	20.1	1.0
	ND2	A:ASN74	4.0	40.0	1.0
	CB	A:ASN74	4.2	35.0	1.0
	CA	A:ALA78	4.3	17.4	1.0
	CG2	A:THR77	4.4	21.5	1.0
	N	A:GLU75	4.5	28.1	1.0
	C	A:GLN76	4.9	24.0	1.0
	CA	A:GLU75	4.9	26.7	1.0
	N	A:GLN76	4.9	23.0	1.0
	C	A:GLU75	4.9	25.0	1.0

Reference:

D.Maruyama, Y.Nishitani, T.Nonaka, A.Kita, T.A.Fukami, T.Mio, H.Yamada-Okabe, T.Yamada-Okabe, K.Miki. Crystal Structure of Uridine-Diphospho-N-Acetylglucosamine Pyrophosphorylase From Candida Albicans and Catalytic Reaction Mechanism J.Biol.Chem. V. 282 17221 2007.
ISSN: ISSN 0021-9258
PubMed: 17392279
DOI: 10.1074/JBC.M611873200

Page generated: Sun Aug 10 16:47:46 2025

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