Bromine in PDB 4gvm: Hiv-1 Integrase Catalytic Core Domain A128T Mutant Complexed with Allosteric Inhibitor

Enzymatic activity of Hiv-1 Integrase Catalytic Core Domain A128T Mutant Complexed with Allosteric Inhibitor

All present enzymatic activity of Hiv-1 Integrase Catalytic Core Domain A128T Mutant Complexed with Allosteric Inhibitor:
2.7.7.49; 2.7.7.7; 3.1.13.2; 3.1.26.13; 3.4.23.16;

Protein crystallography data

The structure of Hiv-1 Integrase Catalytic Core Domain A128T Mutant Complexed with Allosteric Inhibitor, PDB code: 4gvm was solved by L.Feng, M.Kvaratskhelia, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	45.51 / 2.16
*Space group*	P 3₁ 2 1
*Cell size a, b, c (Å), α, β, γ (°)*	72.395, 72.395, 66.165, 90.00, 90.00, 120.00
*R / R_free (%)*	19.9 / 24.9

Other elements in 4gvm:

The structure of Hiv-1 Integrase Catalytic Core Domain A128T Mutant Complexed with Allosteric Inhibitor also contains other interesting chemical elements:

Arsenic	(As)	2 atoms
Chlorine	(Cl)	1 atom

Bromine Binding Sites:

The binding sites of Bromine atom in the Hiv-1 Integrase Catalytic Core Domain A128T Mutant Complexed with Allosteric Inhibitor (pdb code 4gvm). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total only one binding site of Bromine was determined in the Hiv-1 Integrase Catalytic Core Domain A128T Mutant Complexed with Allosteric Inhibitor, PDB code: 4gvm:

Bromine binding site 1 out of 1 in 4gvm

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Bromine Binding Sites List in 4gvm

Bromine binding site 1 out of 1 in the Hiv-1 Integrase Catalytic Core Domain A128T Mutant Complexed with Allosteric Inhibitor

Mono view

Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Hiv-1 Integrase Catalytic Core Domain A128T Mutant Complexed with Allosteric Inhibitor within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Br303 b:58.7 occ:1.00	BR1	A:LF2303	0.0	58.7	1.0
	C1	A:LF2303	1.9	49.0	1.0
	C2	A:LF2303	2.8	46.1	1.0
	C6	A:LF2303	2.8	46.7	1.0
	OG1	A:THR128	3.6	35.7	1.0
	OG1	A:THR124	3.7	50.9	1.0
	CB	A:THR124	3.9	47.3	1.0
	O	A:THR124	4.0	42.8	1.0
	C	A:THR124	4.0	43.5	1.0
	C5	A:LF2303	4.1	41.6	1.0
	C3	A:LF2303	4.1	43.8	1.0
	N	A:THR125	4.2	42.2	1.0
	CA	A:THR125	4.3	42.6	1.0
	CB	A:THR128	4.3	36.6	1.0
	O	A:HOH402	4.6	50.6	1.0
	C4	A:LF2303	4.6	42.9	1.0
	CA	A:THR124	4.6	45.0	1.0
	OG1	A:THR125	4.7	48.6	1.0
	CG2	A:THR128	4.8	38.8	1.0

Reference:

L.Feng, A.Sharma, A.Slaughter, N.Jena, Y.Koh, N.Shkriabai, R.C.Larue, P.A.Patel, H.Mitsuya, J.J.Kessl, A.Engelman, J.R.Fuchs, M.Kvaratskhelia. The A128T Resistance Mutation Reveals Aberrant Protein Multimerization As the Primary Mechanism of Action of Allosteric Hiv-1 Integrase Inhibitors. J.Biol.Chem. V. 288 15813 2013.
ISSN: ISSN 0021-9258
PubMed: 23615903
DOI: 10.1074/JBC.M112.443390

Page generated: Wed Jul 10 21:24:04 2024

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