Fluorine in PDB 2opp: Crystal Structure of Hiv-1 Reverse Transcriptase in Complex with GW420867X.

Enzymatic activity of Crystal Structure of Hiv-1 Reverse Transcriptase in Complex with GW420867X.

All present enzymatic activity of Crystal Structure of Hiv-1 Reverse Transcriptase in Complex with GW420867X.:
2.7.7.49;

Protein crystallography data

The structure of Crystal Structure of Hiv-1 Reverse Transcriptase in Complex with GW420867X., PDB code: 2opp was solved by J.Ren, C.E.Nichols, P.P.Chamberlain, K.L.Weaver, S.J.H.Chan, J.Kleim, D.K.Stammers, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	29.68 / 2.55
*Space group*	P 2₁ 2₁ 2₁
*Cell size a, b, c (Å), α, β, γ (°)*	138.500, 115.300, 65.900, 90.00, 90.00, 90.00
*R / R_free (%)*	20.5 / 29.5

Other elements in 2opp:

The structure of Crystal Structure of Hiv-1 Reverse Transcriptase in Complex with GW420867X. also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Crystal Structure of Hiv-1 Reverse Transcriptase in Complex with GW420867X. (pdb code 2opp). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total only one binding site of Fluorine was determined in the Crystal Structure of Hiv-1 Reverse Transcriptase in Complex with GW420867X., PDB code: 2opp:

Fluorine binding site 1 out of 1 in 2opp

Go back to

Fluorine Binding Sites List in 2opp

Fluorine binding site 1 out of 1 in the Crystal Structure of Hiv-1 Reverse Transcriptase in Complex with GW420867X.

Mono view

Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of Hiv-1 Reverse Transcriptase in Complex with GW420867X. within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:F999 b:39.6 occ:1.00	F1	A:HBQ999	0.0	39.6	1.0
	C7	A:HBQ999	1.3	39.1	1.0
	C8	A:HBQ999	2.3	29.9	1.0
	C6	A:HBQ999	2.3	28.1	1.0
	CD2	A:PHE227	3.3	74.7	1.0
	CB	A:LEU234	3.5	53.8	1.0
	C3	A:HBQ999	3.6	30.8	1.0
	C5	A:HBQ999	3.6	24.3	1.0
	CG1	A:VAL106	3.7	22.2	1.0
	CD1	A:LEU234	3.9	46.1	1.0
	CE2	A:PHE227	4.0	76.0	1.0
	C4	A:HBQ999	4.1	30.7	1.0
	CG	A:PHE227	4.2	67.0	1.0
	CB	A:VAL106	4.2	43.5	1.0
	O	A:LEU234	4.3	57.8	1.0
	CB	A:PHE227	4.3	57.1	1.0
	CG2	A:VAL106	4.3	51.3	1.0
	CG	A:LEU234	4.3	55.1	1.0
	C	A:LEU234	4.4	49.7	1.0
	O	A:HIS235	4.4	65.3	1.0
	CA	A:LEU234	4.6	49.0	1.0
	O2	A:HBQ999	4.8	41.2	1.0
	CD2	A:TYR188	4.8	50.2	1.0
	C	A:HIS235	4.8	56.6	1.0
	N1	A:HBQ999	4.8	41.0	1.0
	N	A:HIS235	4.8	52.9	1.0
	OH	A:TYR318	4.9	37.8	1.0

Reference:

J.Ren, C.E.Nichols, P.P.Chamberlain, K.L.Weaver, S.A.Short, J.H.Chan, J.P.Kleim, D.K.Stammers. Relationship of Potency and Resilience to Drug Resistant Mutations For GW420867X Revealed By Crystal Structures of Inhibitor Complexes For Wild-Type, LEU100ILE, LYS101GLU, and TYR188CYS Mutant Hiv-1 Reverse Transcriptases. J.Med.Chem. V. 50 2301 2007.
ISSN: ISSN 0022-2623
PubMed: 17441703
DOI: 10.1021/JM061117M

Page generated: Wed Jul 31 15:25:32 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0

	© Copyright 2008-2020 by atomistry.com
Home \| Site Map \| Copyright \| Contact us \| Privacy