Chlorine in PDB 1ikv: K103N Mutant Hiv-1 Reverse Transcriptase in Complex with Efivarenz

Enzymatic activity of K103N Mutant Hiv-1 Reverse Transcriptase in Complex with Efivarenz

All present enzymatic activity of K103N Mutant Hiv-1 Reverse Transcriptase in Complex with Efivarenz:
2.7.7.49;

Protein crystallography data

The structure of K103N Mutant Hiv-1 Reverse Transcriptase in Complex with Efivarenz, PDB code: 1ikv was solved by J.Lindberg, T.Unge, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	24.84 / 3.00
*Space group*	C 2 2 2₁
*Cell size a, b, c (Å), α, β, γ (°)*	119.633, 157.168, 156.149, 90.00, 90.00, 90.00
*R / R_free (%)*	22.8 / 29.4

Other elements in 1ikv:

The structure of K103N Mutant Hiv-1 Reverse Transcriptase in Complex with Efivarenz also contains other interesting chemical elements:

Fluorine

(F)

3 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the K103N Mutant Hiv-1 Reverse Transcriptase in Complex with Efivarenz (pdb code 1ikv). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the K103N Mutant Hiv-1 Reverse Transcriptase in Complex with Efivarenz, PDB code: 1ikv:

Chlorine binding site 1 out of 1 in 1ikv

Go back to

Chlorine Binding Sites List in 1ikv

Chlorine binding site 1 out of 1 in the K103N Mutant Hiv-1 Reverse Transcriptase in Complex with Efivarenz

Mono view

Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of K103N Mutant Hiv-1 Reverse Transcriptase in Complex with Efivarenz within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cl2000 b:32.1 occ:1.00	CL	A:EFZ2000	0.0	32.1	1.0
	C4	A:EFZ2000	1.3	34.5	1.0
	C5	A:EFZ2000	2.4	33.4	1.0
	C3	A:EFZ2000	2.4	36.4	1.0
	CB	A:LEU234	3.5	32.0	1.0
	CD2	A:PHE227	3.5	64.0	1.0
	C2	A:EFZ2000	3.7	35.4	1.0
	CG1	A:VAL106	3.7	47.7	1.0
	C6	A:EFZ2000	3.7	32.9	1.0
	CG2	A:VAL106	3.9	45.9	1.0
	C	A:LEU234	3.9	35.1	1.0
	O	A:HIS235	3.9	40.1	1.0
	O	A:LEU234	3.9	35.7	1.0
	C	A:HIS235	4.0	38.1	1.0
	N	A:HIS235	4.1	35.4	1.0
	CE2	A:PHE227	4.2	65.2	1.0
	CG	A:PHE227	4.2	62.2	1.0
	C1	A:EFZ2000	4.2	32.9	1.0
	OH	A:TYR318	4.3	19.8	1.0
	CB	A:PHE227	4.3	58.6	1.0
	CB	A:VAL106	4.3	48.0	1.0
	CA	A:HIS235	4.3	36.5	1.0
	CA	A:LEU234	4.4	33.4	1.0
	N	A:PRO236	4.4	38.2	1.0
	CG	A:LEU234	4.5	30.2	1.0
	CG	A:PRO225	4.7	68.0	1.0
	CB	A:PRO225	4.7	67.5	1.0
	CA	A:PRO236	4.8	38.8	1.0

Reference:

J.Lindberg, S.Sigurdsson, S.Lowgren, H.O.Andersson, C.Sahlberg, R.Noreen, K.Fridborg, H.Zhang, T.Unge. Structural Basis For the Inhibitory Efficacy of Efavirenz (Dmp-266), MSC194 and PNU142721 Towards the Hiv-1 Rt K103N Mutant. Eur.J.Biochem. V. 269 1670 2002.
ISSN: ISSN 0014-2956
PubMed: 11895437
DOI: 10.1046/J.1432-1327.2002.02811.X

Page generated: Fri Jul 19 22:47:18 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW

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