Chlorine in PDB 3ui4: 0.8 A Resolution Crystal Structure of Human Parvulin 14

All present enzymatic activity of 0.8 A Resolution Crystal Structure of Human Parvulin 14:
5.2.1.8;

The structure of 0.8 A Resolution Crystal Structure of Human Parvulin 14, PDB code: 3ui4 was solved by J.W.Mueller, N.M.Link, A.Matena, L.Hoppstock, A.Rueppel, P.Bayer, W.Blankenfeldt, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.80 / 0.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	34.043, 46.966, 51.826, 90.00, 90.00, 90.00
R / Rfree (%)	9.5 / 9.8

The binding sites of Chlorine atom in the 0.8 A Resolution Crystal Structure of Human Parvulin 14 (pdb code 3ui4). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the 0.8 A Resolution Crystal Structure of Human Parvulin 14, PDB code: 3ui4:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the 0.8 A Resolution Crystal Structure of Human Parvulin 14


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of 0.8 A Resolution Crystal Structure of Human Parvulin 14 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl201 b:9.5 occ:0.54 OD1 A:ASP107 2.2 7.5 0.7 CG A:ASP107 2.9 6.9 0.7 O A:HOH445 2.9 16.4 0.5 O A:HOH318 3.2 12.5 1.0 OD2 A:ASP107 3.3 9.5 0.7 HB2 A:ASP107 3.5 3.7 0.3 CB A:ASP107 4.0 6.1 0.7 HB3 A:ASP107 4.0 7.3 0.7 HB2 A:ASP107 4.1 7.3 0.7 CB A:ASP107 4.4 3.1 0.3 HB3 A:ASP107 4.5 3.7 0.3 HH22 A:ARG63 4.5 33.3 0.1 HH21 A:ARG63 4.6 33.3 0.1 OD2 A:ASP107 4.8 7.3 0.3 NH2 A:ARG63 4.9 27.8 0.1 O A:ASP107 5.0 3.6 0.3

Chlorine binding site 2 out of 2 in the 0.8 A Resolution Crystal Structure of Human Parvulin 14


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of 0.8 A Resolution Crystal Structure of Human Parvulin 14 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl202 b:9.7 occ:0.57 H A:LYS119 2.2 6.2 0.3 H A:LYS119 2.3 6.2 0.7 HG3 A:LYS119 2.6 8.9 0.3 O A:HOH412 2.7 30.6 0.9 O A:HOH466 2.8 13.9 0.6 O A:HOH466 2.8 16.7 0.4 HA A:THR118 2.8 4.6 1.0 HB A:THR118 2.9 4.9 1.0 HG22 A:VAL91 3.0 8.7 1.0 HE2 A:LYS119 3.0 10.3 0.3 N A:LYS119 3.0 5.2 0.3 N A:LYS119 3.0 5.2 0.7 HG2 A:LYS119 3.1 8.4 0.7 HD2 A:PRO93 3.1 7.0 1.0 HG21 A:VAL91 3.2 8.7 1.0 HG2 A:PRO93 3.3 7.5 1.0 HE3 A:LYS119 3.4 10.3 0.3 CA A:THR118 3.4 3.8 1.0 CG2 A:VAL91 3.5 7.2 1.0 CG A:LYS119 3.5 7.4 0.3 HB3 A:LYS119 3.5 7.5 0.7 HD3 A:PRO93 3.5 7.0 1.0 CE A:LYS119 3.6 8.6 0.3 CB A:THR118 3.6 4.1 1.0 CD A:PRO93 3.6 5.8 1.0 C A:THR118 3.6 4.6 1.0 HB2 A:LYS119 3.7 7.1 0.3 CG A:PRO93 3.9 6.2 1.0 CG A:LYS119 3.9 7.0 0.7 HG23 A:VAL91 3.9 8.7 1.0 CB A:LYS119 3.9 6.0 0.3 CA A:LYS119 4.0 5.5 0.3 HE3 A:LYS119 4.0 9.9 0.7 CB A:LYS119 4.0 6.3 0.7 HG22 A:THR118 4.1 5.1 1.0 HG2 A:LYS119 4.1 8.9 0.3 CA A:LYS119 4.1 6.2 0.7 CD A:LYS119 4.2 8.5 0.3 HA A:LYS119 4.2 6.6 0.3 HG3 A:PRO93 4.4 7.5 1.0 CG2 A:THR118 4.4 4.3 1.0 HG13 A:VAL91 4.5 8.0 1.0 HE2 A:LYS119 4.5 9.9 0.7 HA A:LYS119 4.6 7.4 0.7 HG11 A:VAL91 4.6 8.0 1.0 HG3 A:LYS119 4.6 8.4 0.7 O A:HOH437 4.6 26.6 0.7 HD3 A:LYS119 4.6 10.2 0.3 CE A:LYS119 4.6 8.2 0.7 O A:HOH341 4.6 29.3 0.9 H A:GLY92 4.7 7.1 1.0 OG1 A:THR118 4.7 4.4 1.0 CB A:VAL91 4.7 6.0 1.0 CD A:LYS119 4.8 8.2 0.7 N A:THR118 4.8 3.6 1.0 CG1 A:VAL91 4.8 6.6 1.0 O A:THR118 4.8 5.1 1.0 HG21 A:THR118 4.9 5.1 1.0 O A:LYS117 4.9 4.8 1.0 HB3 A:LYS119 4.9 7.1 0.3 NZ A:LYS119 4.9 10.0 0.3 HB2 A:PRO93 4.9 6.1 1.0 HB2 A:LYS119 4.9 7.5 0.7 H A:PHE120 5.0 6.5 1.0 HD2 A:LYS119 5.0 10.2 0.3 HZ1 A:LYS119 5.0 12.0 0.3

J.W.Mueller, N.M.Link, A.Matena, L.Hoppstock, A.Ruppel, P.Bayer, W.Blankenfeldt. Crystallographic Proof For An Extended Hydrogen-Bonding Network in Small Prolyl Isomerases. J.Am.Chem.Soc. V. 133 20096 2011.
ISSN: ISSN 0002-7863
PubMed: 22081960
DOI: 10.1021/JA2086195