Sodium in PDB 3nu4: Crystal Structure of Hiv-1 Protease Mutant V32I with Antiviral Drug Amprenavir

Enzymatic activity of Crystal Structure of Hiv-1 Protease Mutant V32I with Antiviral Drug Amprenavir

All present enzymatic activity of Crystal Structure of Hiv-1 Protease Mutant V32I with Antiviral Drug Amprenavir:
3.4.23.16;

Protein crystallography data

The structure of Crystal Structure of Hiv-1 Protease Mutant V32I with Antiviral Drug Amprenavir, PDB code: 3nu4 was solved by Y.-F.Wang, A.Y.Kovalevsky, I.T.Weber, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	10.00 / 1.20
*Space group*	P 2₁ 2₁ 2
*Cell size a, b, c (Å), α, β, γ (°)*	57.769, 86.130, 46.284, 90.00, 90.00, 90.00
*R / R_free (%)*	16.2 / 20

Other elements in 3nu4:

The structure of Crystal Structure of Hiv-1 Protease Mutant V32I with Antiviral Drug Amprenavir also contains other interesting chemical elements:

Chlorine

(Cl)

3 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of Hiv-1 Protease Mutant V32I with Antiviral Drug Amprenavir (pdb code 3nu4). 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 Crystal Structure of Hiv-1 Protease Mutant V32I with Antiviral Drug Amprenavir, PDB code: 3nu4:

Sodium binding site 1 out of 1 in 3nu4

Go back to

Sodium Binding Sites List in 3nu4

Sodium binding site 1 out of 1 in the Crystal Structure of Hiv-1 Protease Mutant V32I with Antiviral Drug Amprenavir

Mono view

Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of Hiv-1 Protease Mutant V32I with Antiviral Drug Amprenavir within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Na500 b:25.5 occ:1.00	O	A:HOH1114	2.3	23.1	1.0
	O	A:HOH1180	2.4	23.1	0.5
	O	A:HOH1058	2.4	23.3	1.0
	O	A:ASP60	2.4	16.5	1.0
	O	A:HOH1082	2.5	26.1	1.0
	O	A:HOH1145	2.5	34.8	1.0
	C	A:ASP60	3.4	16.3	1.0
	N	A:ASP60	3.7	15.2	1.0
	CA	A:ASP60	4.0	16.7	1.0
	O	A:HOH1154	4.2	32.1	0.5
	O	A:ARG41	4.2	20.5	1.0
	CB	A:ASP60	4.3	18.4	1.0
	CB	A:GLN61	4.4	24.5	1.0
	N	A:GLN61	4.5	17.0	1.0
	N	A:ARG41	4.5	22.0	1.0
	O	A:PRO39	4.6	24.0	1.0
	C	A:TYR59	4.7	12.4	1.0
	O	A:GLN61	4.8	21.0	1.0
	CD1	A:ILE62	4.8	15.3	1.0
	CA	A:GLN61	4.8	18.4	1.0
	CA	A:GLY40	4.8	21.6	1.0
	C	A:GLN61	4.8	16.6	1.0
	OE1	A:GLN61	4.9	44.7	1.0
	CG	A:GLN61	4.9	30.7	1.0

Reference:

C.H.Shen, Y.F.Wang, A.Y.Kovalevsky, R.W.Harrison, I.T.Weber. Amprenavir Complexes with Hiv-1 Protease and Its Drug-Resistant Mutants Altering Hydrophobic Clusters. Febs J. V. 277 3699 2010.
ISSN: ISSN 1742-464X
PubMed: 20695887
DOI: 10.1111/J.1742-4658.2010.07771.X

Page generated: Mon Oct 7 11:54:23 2024

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