Magnesium in PDB 3g8d: Crystal Structure of the Biotin Carboxylase Subunit, E296A Mutant, of Acetyl-Coa Carboxylase From Escherichia Coli

Enzymatic activity of Crystal Structure of the Biotin Carboxylase Subunit, E296A Mutant, of Acetyl-Coa Carboxylase From Escherichia Coli

All present enzymatic activity of Crystal Structure of the Biotin Carboxylase Subunit, E296A Mutant, of Acetyl-Coa Carboxylase From Escherichia Coli:
6.3.4.14; 6.4.1.2;

Protein crystallography data

The structure of Crystal Structure of the Biotin Carboxylase Subunit, E296A Mutant, of Acetyl-Coa Carboxylase From Escherichia Coli, PDB code: 3g8d was solved by C.Y.Chou, L.P.Yu, L.Tong, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	30.00 / 1.90
*Space group*	P 2₁ 2₁ 2₁
*Cell size a, b, c (Å), α, β, γ (°)*	81.331, 114.738, 122.148, 90.00, 90.00, 90.00
*R / R_free (%)*	19.8 / 22.6

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Biotin Carboxylase Subunit, E296A Mutant, of Acetyl-Coa Carboxylase From Escherichia Coli (pdb code 3g8d). 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 the Biotin Carboxylase Subunit, E296A Mutant, of Acetyl-Coa Carboxylase From Escherichia Coli, PDB code: 3g8d:

Magnesium binding site 1 out of 1 in 3g8d

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Magnesium Binding Sites List in 3g8d

Magnesium binding site 1 out of 1 in the Crystal Structure of the Biotin Carboxylase Subunit, E296A Mutant, of Acetyl-Coa Carboxylase From Escherichia Coli

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 the Biotin Carboxylase Subunit, E296A Mutant, of Acetyl-Coa Carboxylase From Escherichia Coli within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
B:Mg1002 b:50.8 occ:1.00	O2A	B:ADP1001	1.9	42.4	1.0
	O	B:HOH1493	2.0	39.4	1.0
	O1B	B:ADP1001	2.0	40.2	1.0
	OE2	B:GLU288	2.1	30.4	1.0
	O	B:HOH1538	2.2	37.7	1.0
	PA	B:ADP1001	3.3	41.9	1.0
	CD	B:GLU288	3.3	25.8	1.0
	PB	B:ADP1001	3.3	40.1	1.0
	O3A	B:ADP1001	3.7	41.5	1.0
	OE1	B:GLU288	3.9	31.9	1.0
	O	B:HOH1579	3.9	32.3	1.0
	OE1	B:GLU276	3.9	25.8	1.0
	O2B	B:ADP1001	4.0	40.9	1.0
	C5'	B:ADP1001	4.1	37.1	1.0
	O5'	B:ADP1001	4.2	40.3	1.0
	O	B:HOH1580	4.2	31.2	1.0
	O	B:HOH1485	4.3	36.7	1.0
	O1A	B:ADP1001	4.5	42.6	1.0
	CG	B:GLU288	4.5	24.8	1.0
	O3B	B:ADP1001	4.5	40.3	1.0

Reference:

C.Y.Chou, L.P.Yu, L.Tong. Crystal Structure of Biotin Carboxylase in Complex with Substrates and Implications For Its Catalytic Mechanism. J.Biol.Chem. V. 284 11690 2009.
ISSN: ISSN 0021-9258
PubMed: 19213731
DOI: 10.1074/JBC.M805783200

Page generated: Wed Aug 14 14:41:28 2024

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