Magnesium in PDB 1bpm: Differentiation and Identification of the Two Catalytic Metal Binding Sites in Bovine Lens Leucine Aminopeptidase By X-Ray Crystallography

Enzymatic activity of Differentiation and Identification of the Two Catalytic Metal Binding Sites in Bovine Lens Leucine Aminopeptidase By X-Ray Crystallography

All present enzymatic activity of Differentiation and Identification of the Two Catalytic Metal Binding Sites in Bovine Lens Leucine Aminopeptidase By X-Ray Crystallography:
3.4.11.1;

Protein crystallography data

The structure of Differentiation and Identification of the Two Catalytic Metal Binding Sites in Bovine Lens Leucine Aminopeptidase By X-Ray Crystallography, PDB code: 1bpm was solved by H.Kim, W.N.Lipscomb, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	N/A / 2.90
*Space group*	P 6₃ 2 2
*Cell size a, b, c (Å), α, β, γ (°)*	129.100, 129.100, 120.200, 90.00, 90.00, 120.00
*R / R_free (%)*	18.9 / n/a

Other elements in 1bpm:

The structure of Differentiation and Identification of the Two Catalytic Metal Binding Sites in Bovine Lens Leucine Aminopeptidase By X-Ray Crystallography also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Differentiation and Identification of the Two Catalytic Metal Binding Sites in Bovine Lens Leucine Aminopeptidase By X-Ray Crystallography (pdb code 1bpm). 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 Differentiation and Identification of the Two Catalytic Metal Binding Sites in Bovine Lens Leucine Aminopeptidase By X-Ray Crystallography, PDB code: 1bpm:

Magnesium binding site 1 out of 1 in 1bpm

Go back to

Magnesium Binding Sites List in 1bpm

Magnesium binding site 1 out of 1 in the Differentiation and Identification of the Two Catalytic Metal Binding Sites in Bovine Lens Leucine Aminopeptidase By X-Ray Crystallography

Mono view

Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Differentiation and Identification of the Two Catalytic Metal Binding Sites in Bovine Lens Leucine Aminopeptidase By X-Ray Crystallography within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Mg488 b:4.6 occ:1.00	OD2	A:ASP255	2.2	11.5	1.0
	OE1	A:GLU334	2.2	13.8	1.0
	OD1	A:ASP332	2.2	10.9	1.0
	O	A:ASP332	2.4	7.7	1.0
	ZN	A:ZN489	2.6	16.8	1.0
	CG	A:ASP255	3.2	5.4	1.0
	CG	A:ASP332	3.2	8.6	1.0
	CD	A:GLU334	3.3	15.7	1.0
	C	A:ASP332	3.3	5.9	1.0
	OD1	A:ASP255	3.5	7.9	1.0
	OE2	A:GLU334	3.6	15.8	1.0
	CA	A:ASP332	3.7	5.5	1.0
	NZ	A:LYS262	3.8	9.7	1.0
	CB	A:ASP332	3.9	5.8	1.0
	OD2	A:ASP332	4.1	7.1	1.0
	CE	A:LYS262	4.3	8.0	1.0
	CB	A:ASP255	4.4	2.8	1.0
	OD2	A:ASP273	4.5	5.1	1.0
	NH2	A:ARG336	4.5	21.4	1.0
	N	A:ALA333	4.5	5.3	1.0
	CG	A:GLU334	4.6	8.3	1.0
	N	A:GLU334	4.7	4.7	1.0
	NZ	A:LYS250	4.7	7.0	1.0
	CA	A:ALA333	4.9	2.7	1.0

Reference:

H.Kim, W.N.Lipscomb. Differentiation and Identification of the Two Catalytic Metal Binding Sites in Bovine Lens Leucine Aminopeptidase By X-Ray Crystallography. Proc.Natl.Acad.Sci.Usa V. 90 5006 1993.
ISSN: ISSN 0027-8424
PubMed: 8506345
DOI: 10.1073/PNAS.90.11.5006

Page generated: Mon Dec 14 05:48:05 2020

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