Chlorine in PDB 7lor: X-Ray Radiation Damage Series on Lysozyme at 277K, Multi-Conformer Model, Dataset 3

All present enzymatic activity of X-Ray Radiation Damage Series on Lysozyme at 277K, Multi-Conformer Model, Dataset 3:
3.2.1.17;

The structure of X-Ray Radiation Damage Series on Lysozyme at 277K, Multi-Conformer Model, Dataset 3, PDB code: 7lor was solved by F.Yabukarski, T.Doukov, D.Herschlag, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.61 / 1.52
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	77.397, 77.397, 37.205, 90, 90, 90
R / Rfree (%)	14.5 / 19.7

The structure of X-Ray Radiation Damage Series on Lysozyme at 277K, Multi-Conformer Model, Dataset 3 also contains other interesting chemical elements:

Sodium

(Na)

2 atoms

The binding sites of Chlorine atom in the X-Ray Radiation Damage Series on Lysozyme at 277K, Multi-Conformer Model, Dataset 3 (pdb code 7lor). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the X-Ray Radiation Damage Series on Lysozyme at 277K, Multi-Conformer Model, Dataset 3, PDB code: 7lor:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the X-Ray Radiation Damage Series on Lysozyme at 277K, Multi-Conformer Model, Dataset 3


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of X-Ray Radiation Damage Series on Lysozyme at 277K, Multi-Conformer Model, Dataset 3 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl202 b:24.3 occ:0.49 CL A:CL202 0.0 24.3 0.5 CL A:CL202 1.2 33.7 0.5 HH A:TYR23 2.2 21.7 0.3 HH A:TYR23 2.3 22.3 0.4 HH A:TYR23 2.5 22.7 0.3 OH A:TYR23 2.7 18.1 0.3 OH A:TYR23 2.9 18.6 0.4 OH A:TYR23 3.1 19.0 0.3 HE1 A:TYR23 3.1 19.2 0.3 O A:HOH306 3.2 22.6 0.5 HE1 A:TYR23 3.3 18.5 0.4 HE2 A:TYR23 3.3 17.9 0.3 CZ A:TYR23 3.5 15.5 0.3 HA3 A:GLY104 3.5 22.3 0.3 HA3 A:GLY104 3.6 22.3 0.2 HA3 A:GLY104 3.6 20.9 0.5 CE1 A:TYR23 3.6 16.1 0.3 CZ A:TYR23 3.6 19.0 0.4 CE2 A:TYR23 3.7 14.9 0.3 CZ A:TYR23 3.7 19.1 0.3 CE1 A:TYR23 3.7 15.4 0.4 O A:HOH314 3.9 27.3 0.4 O A:HOH306 3.9 24.6 0.5 HA2 A:GLY104 4.1 22.3 0.2 HA2 A:GLY104 4.2 22.3 0.3 CA A:GLY104 4.2 18.6 0.3 CA A:GLY104 4.3 18.6 0.2 HA2 A:GLY104 4.4 20.9 0.5 CA A:GLY104 4.4 17.5 0.5 O A:ARG21 4.4 23.4 0.4 HH12 A:ARG21 4.5 42.9 0.4 CE1 A:TYR23 4.6 18.7 0.3 O A:ARG21 4.7 23.3 0.3 O A:ARG21 4.8 22.8 0.3 H A:MET105 4.8 20.5 0.3 CD1 A:TYR23 4.8 17.4 0.3 CE2 A:TYR23 4.8 16.8 0.4 H A:MET105 4.8 20.8 0.2 N A:GLY104 4.9 18.3 0.3 HE1 A:TYR23 4.9 22.4 0.3 CD2 A:TYR23 4.9 17.6 0.3 CE2 A:TYR23 4.9 16.9 0.3 H A:MET105 4.9 21.2 0.5 NH1 A:ARG21 4.9 35.8 0.4 HH11 A:ARG21 4.9 42.9 0.4 CD1 A:TYR23 5.0 16.4 0.4 HB3 A:ARG21 5.0 26.6 0.3 HB3 A:ARG21 5.0 29.6 0.4 N A:GLY104 5.0 20.5 0.2

Chlorine binding site 2 out of 2 in the X-Ray Radiation Damage Series on Lysozyme at 277K, Multi-Conformer Model, Dataset 3


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of X-Ray Radiation Damage Series on Lysozyme at 277K, Multi-Conformer Model, Dataset 3 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl202 b:33.7 occ:0.51 CL A:CL202 0.0 33.7 0.5 CL A:CL202 1.2 24.3 0.5 HH A:TYR23 2.0 21.7 0.3 HH A:TYR23 2.3 22.3 0.4 HH A:TYR23 2.5 22.7 0.3 HA3 A:GLY104 2.7 22.3 0.3 OH A:TYR23 2.8 18.1 0.3 O A:HOH314 2.8 27.3 0.4 HA3 A:GLY104 2.8 22.3 0.2 HA3 A:GLY104 2.8 20.9 0.5 HE1 A:TYR23 2.9 19.2 0.3 HE2 A:TYR23 2.9 17.9 0.3 HE1 A:TYR23 3.0 18.5 0.4 OH A:TYR23 3.0 18.6 0.4 HA2 A:GLY104 3.1 22.3 0.2 HA2 A:GLY104 3.1 22.3 0.3 OH A:TYR23 3.2 19.0 0.3 CA A:GLY104 3.3 18.6 0.3 HA2 A:GLY104 3.4 20.9 0.5 CA A:GLY104 3.4 18.6 0.2 CE2 A:TYR23 3.5 14.9 0.3 CA A:GLY104 3.5 17.5 0.5 CZ A:TYR23 3.5 15.5 0.3 CE1 A:TYR23 3.6 16.1 0.3 CE1 A:TYR23 3.7 15.4 0.4 CZ A:TYR23 3.8 19.0 0.4 CZ A:TYR23 3.8 19.1 0.3 N A:GLY104 3.9 18.3 0.3 O A:HOH306 4.0 22.6 0.5 H A:GLY104 4.0 21.9 0.2 HH12 A:ARG21 4.0 42.9 0.4 N A:GLY104 4.1 19.7 0.5 N A:GLY104 4.1 20.5 0.2 H A:GLY104 4.2 23.6 0.3 H A:GLY104 4.3 24.6 0.2 O A:HOH314 4.3 29.5 0.6 NH1 A:ARG21 4.4 35.8 0.4 H A:MET105 4.4 20.5 0.3 H A:MET105 4.4 20.8 0.2 HB3 A:ARG21 4.4 29.6 0.4 H A:MET105 4.5 21.2 0.5 O A:ARG21 4.5 23.4 0.4 HH11 A:ARG21 4.5 42.9 0.4 HB3 A:ARG21 4.6 26.6 0.3 C A:ASN103 4.6 20.4 0.2 C A:GLY104 4.6 17.9 0.3 C A:GLY104 4.7 18.1 0.2 HB3 A:ARG21 4.7 29.4 0.3 C A:ASN103 4.8 19.8 0.3 CD2 A:TYR23 4.8 17.6 0.3 O A:GLY102 4.8 34.3 0.4 O A:HOH306 4.8 24.6 0.5 CD1 A:TYR23 4.8 17.4 0.3 HG22 A:VAL99 4.8 23.1 0.4 C A:ASN103 4.8 20.4 0.2 C A:GLY104 4.8 17.6 0.5 O A:ASN103 4.8 20.3 0.3 O A:ARG21 4.8 22.8 0.3 CE1 A:TYR23 4.8 18.7 0.3 C A:ASN103 4.8 19.6 0.3 HG22 A:VAL99 4.8 22.8 0.2 N A:MET105 4.9 17.1 0.7 O A:VAL99 4.9 19.8 0.4 N A:MET105 4.9 17.4 0.2 O A:ASN103 4.9 20.8 0.2 O A:VAL99 4.9 25.6 0.4 CD1 A:TYR23 4.9 16.4 0.4 O A:ARG21 4.9 23.3 0.3 HG22 A:VAL99 5.0 22.6 0.4 N A:MET105 5.0 17.7 0.1 O A:VAL99 5.0 25.7 0.2 HD1 A:TYR23 5.0 20.9 0.3

F.Yabukarski, T.Doukov, D.A.Mokhtari, S.Du, D.Herschlag. Evaluating the Impact of X-Ray Damage on Conformational Heterogeneity in Room-Temperature (277 K) and Cryo-Cooled Protein Crystals. Acta Crystallogr D Struct V. 78 945 2022BIOL.
ISSN: ISSN 2059-7983
PubMed: 35916220
DOI: 10.1107/S2059798322005939