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

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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: Mon Jul 14 13:53:50 2025

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