Magnesium in PDB 5ls7: Complex of Wild Type E. Coli Alpha Aspartate Decarboxylase with Its Processing Factor Panz

Enzymatic activity of Complex of Wild Type E. Coli Alpha Aspartate Decarboxylase with Its Processing Factor Panz

All present enzymatic activity of Complex of Wild Type E. Coli Alpha Aspartate Decarboxylase with Its Processing Factor Panz:
4.1.1.11;

Protein crystallography data

The structure of Complex of Wild Type E. Coli Alpha Aspartate Decarboxylase with Its Processing Factor Panz, PDB code: 5ls7 was solved by D.C.F.Monteiro, M.E.Webb, A.R.Pearson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	29.28 / 1.16
*Space group*	I 4
*Cell size a, b, c (Å), α, β, γ (°)*	85.863, 85.863, 80.055, 90.00, 90.00, 90.00
*R / R_free (%)*	11.3 / 13.7

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Complex of Wild Type E. Coli Alpha Aspartate Decarboxylase with Its Processing Factor Panz (pdb code 5ls7). 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 Complex of Wild Type E. Coli Alpha Aspartate Decarboxylase with Its Processing Factor Panz, PDB code: 5ls7:

Magnesium binding site 1 out of 1 in 5ls7

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Magnesium Binding Sites List in 5ls7

Magnesium binding site 1 out of 1 in the Complex of Wild Type E. Coli Alpha Aspartate Decarboxylase with Its Processing Factor Panz

Mono view

Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Complex of Wild Type E. Coli Alpha Aspartate Decarboxylase with Its Processing Factor Panz within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
B:Mg204 b:16.7 occ:1.00	O5A	B:ACO203	2.7	10.7	1.0
	O	B:THR72	2.8	12.0	1.0
	N	B:ARG75	2.8	11.0	1.0
	N	B:VAL77	3.0	9.7	1.0
	N	B:GLY76	3.2	10.2	1.0
	CA	B:ARG75	3.3	11.5	0.5
	CB	B:VAL77	3.4	9.9	1.0
	C	B:ARG75	3.4	11.0	1.0
	N	B:ARG74	3.4	11.5	1.0
	CA	B:ARG75	3.4	11.4	0.5
	CG2	B:VAL77	3.4	11.0	1.0
	CB	B:ARG75	3.5	13.5	0.5
	C	B:ARG73	3.6	11.5	1.0
	O1A	B:ACO203	3.7	11.9	1.0
	CA	B:ARG73	3.7	11.3	1.0
	P2A	B:ACO203	3.7	10.9	1.0
	CA	B:VAL77	3.7	9.8	1.0
	CB	B:ARG75	3.7	9.6	0.5
	C	B:THR72	3.8	10.8	1.0
	O4A	B:ACO203	3.9	11.3	1.0
	C	B:ARG74	3.9	12.0	1.0
	C	B:GLY76	4.0	10.0	1.0
	CA	B:ARG74	4.1	12.1	1.0
	CA	B:GLY76	4.1	10.8	1.0
	O	B:ARG75	4.1	14.0	1.0
	N	B:ARG73	4.2	11.2	1.0
	N	B:GLY78	4.3	9.5	1.0
	O	B:ARG73	4.3	12.9	1.0
	CG1	B:VAL68	4.3	10.8	1.0
	P1A	B:ACO203	4.4	11.2	1.0
	CG	B:ARG75	4.5	13.5	0.5
	O3A	B:ACO203	4.5	11.3	1.0
	C	B:VAL77	4.6	9.3	1.0
	O2A	B:ACO203	4.7	11.4	1.0
	CG1	B:VAL77	4.7	10.8	1.0
	CG	B:ARG75	4.7	11.2	0.5
	OG1	B:THR72	4.8	11.1	1.0
	CB	B:ARG73	4.9	11.5	1.0

Reference:

Z.L.P.Arnott, S.Nozaki, D.C.F.Monteiro, H.E.Morgan, A.R.Pearson, H.Niki, M.E.Webb. The Mechanism of Regulation of Pantothenate Biosynthesis By the Pand-Panzaccoa Complex Reveals An Additional Mode of Action For the Antimetabolite N-Pentyl Pantothenamide (N5-Pan). Biochemistry V. 56 4931 2017.
ISSN: ISSN 1520-4995
PubMed: 28832133
DOI: 10.1021/ACS.BIOCHEM.7B00509

Page generated: Sun Sep 29 20:35:44 2024

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