Sodium in PDB 2anp: Functional Glutamate 151 to Histidine Mutant of the Aminopeptidase From Aeromonas Proteolytica.

Enzymatic activity of Functional Glutamate 151 to Histidine Mutant of the Aminopeptidase From Aeromonas Proteolytica.

All present enzymatic activity of Functional Glutamate 151 to Histidine Mutant of the Aminopeptidase From Aeromonas Proteolytica.:
3.4.11.10;

Protein crystallography data

The structure of Functional Glutamate 151 to Histidine Mutant of the Aminopeptidase From Aeromonas Proteolytica., PDB code: 2anp was solved by K.P.Bzymek, A.Moulin, S.I.Swierczek, D.Ringe, G.A.Petsko, R.C.Holz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	50.00 / 1.90
*Space group*	P 6₁ 2 2
*Cell size a, b, c (Å), α, β, γ (°)*	109.090, 109.090, 98.417, 90.00, 90.00, 120.00
*R / R_free (%)*	18 / 20.5

Other elements in 2anp:

The structure of Functional Glutamate 151 to Histidine Mutant of the Aminopeptidase From Aeromonas Proteolytica. also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Functional Glutamate 151 to Histidine Mutant of the Aminopeptidase From Aeromonas Proteolytica. (pdb code 2anp). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Functional Glutamate 151 to Histidine Mutant of the Aminopeptidase From Aeromonas Proteolytica., PDB code: 2anp:

Sodium binding site 1 out of 1 in 2anp

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Sodium Binding Sites List in 2anp

Sodium binding site 1 out of 1 in the Functional Glutamate 151 to Histidine Mutant of the Aminopeptidase From Aeromonas Proteolytica.

Mono view

Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Functional Glutamate 151 to Histidine Mutant of the Aminopeptidase From Aeromonas Proteolytica. within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Na503 b:31.6 occ:1.00	O	A:HOH534	2.3	26.1	1.0
	OH	A:TYR218	2.4	20.6	1.0
	O	A:HOH606	2.5	43.8	1.0
	O	A:HOH617	2.6	44.2	1.0
	CZ	A:TYR218	3.4	19.8	1.0
	CE1	A:TYR218	3.6	18.6	1.0
	OD2	A:ASP210	4.2	24.9	1.0
	OG1	A:THR206	4.2	18.8	1.0
	CB	A:THR206	4.4	19.1	1.0
	OD1	A:ASP210	4.7	24.8	1.0
	CE2	A:TYR218	4.7	19.4	1.0
	NE2	A:GLN203	4.8	22.9	1.0
	CG	A:ASP210	4.9	23.5	1.0
	O	A:HOH638	4.9	40.3	1.0
	CD1	A:TYR218	5.0	17.5	1.0

Reference:

K.P.Bzymek, A.Moulin, S.I.Swierczek, D.Ringe, G.A.Petsko, B.Bennett, R.C.Holz. Kinetic, Spectroscopic, and X-Ray Crystallographic Characterization of the Functional E151H Aminopeptidase From Aeromonas Proteolytica. Biochemistry V. 44 12030 2005.
ISSN: ISSN 0006-2960
PubMed: 16142900
DOI: 10.1021/BI0505823

Page generated: Mon Oct 7 01:52:49 2024

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