Chlorine in PDB 7loq: X-Ray Radiation Damage Series on Lysozyme at 277K, Multi-Conformer Model, Dataset 2

All present enzymatic activity of X-Ray Radiation Damage Series on Lysozyme at 277K, Multi-Conformer Model, Dataset 2:
3.2.1.17;

The structure of X-Ray Radiation Damage Series on Lysozyme at 277K, Multi-Conformer Model, Dataset 2, PDB code: 7loq 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)	34.54 / 1.30
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	77.223, 77.223, 37.188, 90, 90, 90
R / Rfree (%)	13.8 / 16.9

The structure of X-Ray Radiation Damage Series on Lysozyme at 277K, Multi-Conformer Model, Dataset 2 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 2 (pdb code 7loq). 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 2, PDB code: 7loq:
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 2


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 2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl202 b:21.3 occ:0.54 CL A:CL202 0.0 21.3 0.5 CL A:CL202 1.2 26.7 0.5 HH A:TYR23 2.1 17.2 0.3 HH A:TYR23 2.3 16.6 0.3 HH A:TYR23 2.6 16.5 0.3 OH A:TYR23 2.7 14.4 0.3 OH A:TYR23 2.8 13.8 0.3 HE1 A:TYR23 3.2 16.6 0.3 OH A:TYR23 3.2 13.7 0.3 O A:HOH306 3.2 18.6 0.5 HE1 A:TYR23 3.2 14.6 0.3 HE2 A:TYR23 3.3 14.3 0.3 HA3 A:GLY104 3.4 14.6 0.4 CZ A:TYR23 3.4 13.5 0.3 HA3 A:GLY104 3.5 18.2 0.1 CZ A:TYR23 3.6 12.4 0.3 HA3 A:GLY104 3.6 17.8 0.5 CE2 A:TYR23 3.7 11.9 0.3 CE1 A:TYR23 3.7 13.8 0.3 CE1 A:TYR23 3.7 12.2 0.3 O A:HOH313 3.7 23.3 0.4 CZ A:TYR23 3.7 11.7 0.3 HA2 A:GLY104 4.0 18.2 0.1 HA2 A:GLY104 4.1 14.6 0.4 CA A:GLY104 4.1 12.2 0.4 O A:HOH306 4.1 22.9 0.5 CA A:GLY104 4.2 15.2 0.1 HA2 A:GLY104 4.4 17.8 0.5 CA A:GLY104 4.4 14.8 0.5 O A:ARG21 4.4 17.1 0.3 CE1 A:TYR23 4.5 11.2 0.3 O A:ARG21 4.7 15.5 0.3 HH12 A:ARG21 4.7 35.3 0.3 O A:ARG21 4.7 18.3 0.3 N A:GLY104 4.7 15.0 0.4 HE1 A:TYR23 4.7 13.4 0.3 H A:MET105 4.7 15.2 0.1 CE2 A:TYR23 4.8 11.4 0.3 H A:MET105 4.8 16.1 0.4 H A:MET105 4.8 15.0 0.5 CD1 A:TYR23 4.8 12.9 0.3 CD2 A:TYR23 4.9 12.9 0.3 CD1 A:TYR23 4.9 13.0 0.3 N A:GLY104 4.9 17.2 0.1 HB3 A:ARG21 4.9 25.7 0.3 HB3 A:ARG21 4.9 20.7 0.3 H A:GLY104 4.9 18.0 0.2 CE2 A:TYR23 4.9 12.6 0.3

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


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 2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl202 b:26.7 occ:0.46 CL A:CL202 0.0 26.7 0.5 CL A:CL202 1.2 21.3 0.5 HH A:TYR23 1.9 17.2 0.3 HH A:TYR23 2.2 16.6 0.3 HH A:TYR23 2.6 16.5 0.3 O A:HOH313 2.6 23.3 0.4 HA3 A:GLY104 2.7 14.6 0.4 OH A:TYR23 2.7 14.4 0.3 HA3 A:GLY104 2.8 18.2 0.1 HA3 A:GLY104 2.9 17.8 0.5 HE2 A:TYR23 2.9 14.3 0.3 HE1 A:TYR23 2.9 16.6 0.3 HE1 A:TYR23 2.9 14.6 0.3 OH A:TYR23 3.0 13.8 0.3 HA2 A:GLY104 3.0 18.2 0.1 HA2 A:GLY104 3.1 14.6 0.4 CA A:GLY104 3.3 12.2 0.4 CA A:GLY104 3.3 15.2 0.1 OH A:TYR23 3.4 13.7 0.3 HA2 A:GLY104 3.4 17.8 0.5 CE2 A:TYR23 3.5 11.9 0.3 CZ A:TYR23 3.5 13.5 0.3 CA A:GLY104 3.5 14.8 0.5 CE1 A:TYR23 3.6 12.2 0.3 CE1 A:TYR23 3.6 13.8 0.3 CZ A:TYR23 3.8 12.4 0.3 N A:GLY104 3.8 15.0 0.4 H A:GLY104 3.9 18.0 0.2 O A:HOH306 3.9 18.6 0.5 CZ A:TYR23 3.9 11.7 0.3 N A:GLY104 4.0 17.2 0.1 N A:GLY104 4.1 17.7 0.5 O A:HOH313 4.2 23.5 0.6 HH12 A:ARG21 4.2 35.3 0.3 H A:GLY104 4.2 20.6 0.2 H A:GLY104 4.3 21.2 0.3 HB3 A:ARG21 4.3 25.7 0.3 H A:MET105 4.4 15.2 0.1 H A:MET105 4.4 15.0 0.5 O A:ARG21 4.4 17.1 0.3 NH1 A:ARG21 4.4 29.4 0.3 H A:MET105 4.5 16.1 0.4 HB3 A:ARG21 4.5 20.7 0.3 C A:ASN103 4.6 15.6 0.2 HB3 A:ARG21 4.6 25.9 0.3 HH11 A:ARG21 4.6 35.3 0.3 C A:GLY104 4.6 14.5 0.1 C A:GLY104 4.6 14.1 0.4 C A:ASN103 4.6 15.8 0.3 O A:ASN103 4.7 15.9 0.3 HG22 A:VAL99 4.7 20.1 0.4 O A:ARG21 4.7 18.3 0.3 CD2 A:TYR23 4.7 12.9 0.3 HG22 A:VAL99 4.8 19.4 0.3 CE1 A:TYR23 4.8 11.2 0.3 CD1 A:TYR23 4.8 12.9 0.3 C A:GLY104 4.8 12.7 0.5 C A:ASN103 4.8 16.5 0.2 C A:ASN103 4.8 15.8 0.3 O A:VAL99 4.9 19.5 0.3 O A:ARG21 4.9 15.5 0.3 N A:MET105 4.9 12.6 0.2 O A:VAL99 4.9 15.6 0.4 O A:VAL99 4.9 18.3 0.3 CD1 A:TYR23 4.9 13.0 0.3 O A:ASN103 4.9 15.8 0.2 N A:MET105 4.9 13.4 0.4 N A:MET105 4.9 12.5 0.3 O A:GLY102 5.0 26.4 0.5 HG22 A:VAL99 5.0 18.6 0.3 HD1 A:TYR23 5.0 15.5 0.3 O A:HOH306 5.0 22.9 0.5

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