Chlorine in PDB 1ezf: Crystal Structure of Human Squalene Synthase

All present enzymatic activity of Crystal Structure of Human Squalene Synthase:
2.5.1.21;

The structure of Crystal Structure of Human Squalene Synthase, PDB code: 1ezf was solved by J.Pandit, D.E.Danley, G.K.Schulte, S.M.Mazzalupo, T.A.Pauly, C.M.Hayward, E.S.Hamanaka, J.F.Thompson, H.J.Harwood, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.00 / 2.15
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	76.760, 87.920, 154.170, 90.00, 90.00, 90.00
R / Rfree (%)	21.3 / 26.2

The binding sites of Chlorine atom in the Crystal Structure of Human Squalene Synthase (pdb code 1ezf). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Crystal Structure of Human Squalene Synthase, PDB code: 1ezf:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Crystal Structure of Human Squalene Synthase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Human Squalene Synthase within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl991 b:23.8 occ:1.00 CL36 A:IN0991 0.0 23.8 1.0 C20 A:IN0991 1.7 23.0 1.0 C9 A:IN0991 2.7 24.5 1.0 C21 A:IN0991 2.7 25.9 1.0 CD2 A:PHE72 3.9 24.4 1.0 CD2 A:LEU183 3.9 14.1 1.0 CA A:TYR73 4.0 24.7 1.0 CB A:TYR73 4.0 23.2 1.0 C8 A:IN0991 4.0 21.7 1.0 N A:TYR73 4.0 24.9 1.0 C1 A:IN0991 4.0 26.6 1.0 CD1 A:LEU76 4.1 16.5 1.0 CD1 A:LEU183 4.1 19.0 1.0 CD2 A:TYR73 4.3 21.6 1.0 CG A:LEU183 4.3 17.1 1.0 CG1 A:VAL69 4.3 22.8 1.0 CG A:PHE72 4.4 25.8 1.0 CG1 A:VAL179 4.4 24.0 1.0 O A:VAL69 4.5 23.4 1.0 CB A:PHE72 4.5 22.3 1.0 CE2 A:PHE72 4.5 28.0 1.0 C A:PHE72 4.5 24.8 1.0 C2 A:IN0991 4.5 25.9 1.0 CZ A:PHE288 4.6 20.9 1.0 CG A:TYR73 4.6 25.4 1.0 O A:PHE72 4.9 23.8 1.0

Chlorine binding site 2 out of 3 in the Crystal Structure of Human Squalene Synthase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Human Squalene Synthase within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl992 b:17.5 occ:1.00 CL36 B:IN0992 0.0 17.5 1.0 C20 B:IN0992 1.7 17.5 1.0 C9 B:IN0992 2.7 16.9 1.0 C21 B:IN0992 2.7 17.8 1.0 CD1 B:LEU183 3.9 9.1 1.0 CD2 B:LEU183 3.9 5.6 1.0 CD1 B:LEU76 3.9 13.2 1.0 C8 B:IN0992 4.0 18.1 1.0 C1 B:IN0992 4.1 17.1 1.0 CG1 B:VAL179 4.1 11.9 1.0 CD2 B:PHE72 4.1 7.9 1.0 CD2 B:TYR73 4.1 16.9 1.0 CG B:LEU183 4.2 9.8 1.0 CA B:TYR73 4.2 12.4 1.0 CB B:TYR73 4.3 15.7 1.0 N B:TYR73 4.3 13.5 1.0 CG1 B:VAL69 4.5 13.4 1.0 C2 B:IN0992 4.6 18.5 1.0 CZ B:PHE288 4.6 12.8 1.0 CE2 B:PHE72 4.6 6.7 1.0 O B:VAL69 4.7 17.2 1.0 CG B:TYR73 4.7 17.9 1.0 CG B:PHE72 4.7 13.1 1.0 CB B:PHE72 4.9 9.5 1.0 C B:PHE72 4.9 12.2 1.0

Chlorine binding site 3 out of 3 in the Crystal Structure of Human Squalene Synthase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of Human Squalene Synthase within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl995 b:24.9 occ:1.00 CL36 C:IN0995 0.0 24.9 1.0 C20 C:IN0995 1.7 25.3 1.0 C9 C:IN0995 2.7 27.6 1.0 C21 C:IN0995 2.7 24.8 1.0 CD2 C:LEU183 3.6 19.3 1.0 CD2 C:PHE72 4.0 19.6 1.0 CA C:TYR73 4.0 19.3 1.0 CB C:TYR73 4.0 17.7 1.0 C8 C:IN0995 4.0 25.4 1.0 C1 C:IN0995 4.0 25.7 1.0 CD1 C:LEU76 4.0 16.1 1.0 CD2 C:TYR73 4.0 20.0 1.0 N C:TYR73 4.1 20.0 1.0 CG1 C:VAL69 4.1 15.1 1.0 O C:VAL69 4.3 20.4 1.0 CG C:LEU183 4.3 21.7 1.0 CD1 C:LEU183 4.3 20.0 1.0 CZ C:PHE288 4.4 24.5 1.0 CG1 C:VAL179 4.5 19.7 1.0 CG C:TYR73 4.5 20.5 1.0 C2 C:IN0995 4.5 25.3 1.0 CE2 C:PHE72 4.6 25.5 1.0 CG C:PHE72 4.6 19.4 1.0 C C:PHE72 4.6 17.4 1.0 CB C:PHE72 4.7 16.2 1.0

J.Pandit, D.E.Danley, G.K.Schulte, S.Mazzalupo, T.A.Pauly, C.M.Hayward, E.S.Hamanaka, J.F.Thompson, H.J.Harwood Jr.. Crystal Structure of Human Squalene Synthase. A Key Enzyme in Cholesterol Biosynthesis. J.Biol.Chem. V. 275 30610 2000.
ISSN: ISSN 0021-9258
PubMed: 10896663
DOI: 10.1074/JBC.M004132200