Fluorine in PDB 7trm: Crystal Structure of Human BIRC2 BIR3 Domain in Complex with Inhibitor Lcl-161

Enzymatic activity of Crystal Structure of Human BIRC2 BIR3 Domain in Complex with Inhibitor Lcl-161

All present enzymatic activity of Crystal Structure of Human BIRC2 BIR3 Domain in Complex with Inhibitor Lcl-161:
2.3.2.27;

Protein crystallography data

The structure of Crystal Structure of Human BIRC2 BIR3 Domain in Complex with Inhibitor Lcl-161, PDB code: 7trm was solved by A.H.Tencer, B.J.Klein, T.G.Kutateladze, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 27.13 / 2.40
Space group P 3 2 1
Cell size a, b, c (Å), α, β, γ (°) 104.71, 104.71, 27.132, 90, 90, 120
R / Rfree (%) 17.4 / 22.5

Other elements in 7trm:

The structure of Crystal Structure of Human BIRC2 BIR3 Domain in Complex with Inhibitor Lcl-161 also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Crystal Structure of Human BIRC2 BIR3 Domain in Complex with Inhibitor Lcl-161 (pdb code 7trm). 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 Human BIRC2 BIR3 Domain in Complex with Inhibitor Lcl-161, PDB code: 7trm:

Fluorine binding site 1 out of 1 in 7trm

Go back to Fluorine Binding Sites List in 7trm
Fluorine binding site 1 out of 1 in the Crystal Structure of Human BIRC2 BIR3 Domain in Complex with Inhibitor Lcl-161


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 Human BIRC2 BIR3 Domain in Complex with Inhibitor Lcl-161 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F405

b:41.0
occ:1.00
 F02 A:IUN405 0.0 41.0 1.0
C35 A:IUN405 1.4 36.0 1.0
C33 A:IUN405 2.3 37.2 1.0
C34 A:IUN405 2.3 34.6 1.0
O A:VAL304 3.4 29.2 1.0
CB A:ASP303 3.4 34.4 1.0
CG A:LYS305 3.4 33.2 1.0
CG1 A:VAL298 3.6 27.9 1.0
C32 A:IUN405 3.6 38.5 1.0
C31 A:IUN405 3.6 34.7 1.0
CE A:LYS305 3.7 43.0 1.0
C A:VAL304 3.8 31.2 1.0
N A:VAL304 3.8 28.6 1.0
C A:ASP303 4.0 32.3 1.0
CG A:ASP303 4.0 34.9 1.0
C30 A:IUN405 4.1 41.3 1.0
OD2 A:ASP303 4.1 38.2 1.0
CA A:ASP303 4.1 32.9 1.0
CD A:LYS305 4.2 40.8 1.0
CA A:VAL304 4.3 29.4 1.0
CG2 A:VAL298 4.3 32.8 1.0
N A:LYS305 4.4 29.2 1.0
O A:HOH505 4.4 39.1 1.0
CA A:GLY312 4.4 32.4 1.0
CB A:VAL298 4.5 32.5 1.0
O A:ASP303 4.6 32.5 1.0
CB A:LYS305 4.6 30.7 1.0
CA A:LYS305 4.8 31.4 1.0
OD1 A:ASP303 4.8 33.9 1.0
N A:LEU313 4.9 32.0 1.0
O A:LEU313 4.9 33.9 1.0

Reference:

A.H.Tencer, Y.Yu, S.Z.Causse, G.R.Campbell, B.J.Klein, H.Xuan, J.Cartier, M.A.Miles, N.Gaurav, A.Zadoroznyj, T.A.Holt, H.Wen, C.J.Hawkins, S.A.Spector, L.Dubrez, X.Shi, T.G.Kutateladze. Molecular Basis For Nuclear Accumulation and Targeting of the Inhibitor of Apoptosis BIRC2 Nat.Struct.Mol.Biol. 2023.
ISSN: ESSN 1545-9985
DOI: 10.1038/S41594-023-01044-1
Page generated: Fri Aug 2 13:38:54 2024

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