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

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

The structure of X-Ray Radiation Damage Series on Lysozyme at 277K, Multi-Conformer Model, Dataset 3 (Merged), PDB code: 7lpl 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)	34.55 / 1.14
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	77.26, 77.26, 37.26, 90, 90, 90
R / Rfree (%)	13.7 / 15.8

The structure of X-Ray Radiation Damage Series on Lysozyme at 277K, Multi-Conformer Model, Dataset 3 (Merged) 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 (Merged) (pdb code 7lpl). 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 (Merged), PDB code: 7lpl:
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 (Merged)


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 (Merged) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl202 b:20.7 occ:0.52 CL A:CL202 0.0 20.7 0.5 CL A:CL202 1.1 25.0 0.5 HH A:TYR23 2.2 17.7 0.3 HH A:TYR23 2.2 16.3 0.3 HH A:TYR23 2.5 18.4 0.3 OH A:TYR23 2.8 13.6 0.3 OH A:TYR23 2.8 14.7 0.3 HE1 A:TYR23 3.0 16.6 0.3 OH A:TYR23 3.1 15.3 0.3 O A:HOH308 3.2 19.3 0.5 HE1 A:TYR23 3.2 13.7 0.3 HA3 A:GLY104 3.3 15.5 0.3 HE2 A:TYR23 3.4 15.4 0.3 CZ A:TYR23 3.5 12.7 0.3 HA3 A:GLY104 3.5 19.7 0.2 CZ A:TYR23 3.6 11.0 0.3 CE1 A:TYR23 3.6 13.9 0.3 HA3 A:GLY104 3.6 19.1 0.5 CZ A:TYR23 3.7 12.1 0.3 CE1 A:TYR23 3.7 11.4 0.3 CE2 A:TYR23 3.7 12.8 0.3 O A:HOH315 3.7 22.6 0.4 HA2 A:GLY104 4.0 19.7 0.2 HA2 A:GLY104 4.1 15.5 0.3 CA A:GLY104 4.1 12.9 0.3 O A:HOH308 4.1 22.0 0.5 CA A:GLY104 4.2 16.4 0.2 O A:ARG21 4.4 19.2 0.3 CA A:GLY104 4.5 15.9 0.5 HA2 A:GLY104 4.5 19.1 0.5 CE1 A:TYR23 4.6 11.9 0.3 O A:ARG21 4.6 17.3 0.3 N A:GLY104 4.7 12.9 0.3 HH12 A:ARG21 4.7 28.7 0.3 CE2 A:TYR23 4.7 12.4 0.3 H A:MET105 4.7 15.2 0.2 CD1 A:TYR23 4.7 12.4 0.3 H A:MET105 4.8 14.0 0.5 O A:ARG21 4.8 16.7 0.3 H A:MET105 4.8 15.4 0.3 HE1 A:TYR23 4.8 14.3 0.3 H A:GLY104 4.8 15.5 0.2 CE2 A:TYR23 4.9 15.2 0.3 CD2 A:TYR23 4.9 13.5 0.3 N A:GLY104 4.9 15.4 0.2 HB3 A:ARG21 4.9 20.1 0.3 CD1 A:TYR23 4.9 13.4 0.3 HB3 A:ARG21 5.0 24.8 0.3

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


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 (Merged) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl202 b:25.0 occ:0.48 CL A:CL202 0.0 25.0 0.5 CL A:CL202 1.1 20.7 0.5 HH A:TYR23 2.0 16.3 0.3 HH A:TYR23 2.1 17.7 0.3 HH A:TYR23 2.5 18.4 0.3 HA3 A:GLY104 2.6 15.5 0.3 O A:HOH315 2.7 22.6 0.4 OH A:TYR23 2.8 13.6 0.3 HE1 A:TYR23 2.8 16.6 0.3 HA3 A:GLY104 2.8 19.7 0.2 HA3 A:GLY104 2.9 19.1 0.5 OH A:TYR23 2.9 14.7 0.3 HE2 A:TYR23 3.0 15.4 0.3 HE1 A:TYR23 3.0 13.7 0.3 HA2 A:GLY104 3.1 19.7 0.2 HA2 A:GLY104 3.1 15.5 0.3 CA A:GLY104 3.2 12.9 0.3 OH A:TYR23 3.3 15.3 0.3 CA A:GLY104 3.4 16.4 0.2 HA2 A:GLY104 3.5 19.1 0.5 CE2 A:TYR23 3.5 12.8 0.3 CE1 A:TYR23 3.5 13.9 0.3 CZ A:TYR23 3.5 12.7 0.3 CA A:GLY104 3.6 15.9 0.5 CE1 A:TYR23 3.6 11.4 0.3 N A:GLY104 3.7 12.9 0.3 CZ A:TYR23 3.7 11.0 0.3 H A:GLY104 3.8 15.5 0.2 CZ A:TYR23 3.8 12.1 0.3 O A:HOH308 4.0 19.3 0.5 N A:GLY104 4.0 15.4 0.2 O A:HOH315 4.2 24.1 0.6 N A:GLY104 4.2 16.3 0.5 H A:GLY104 4.2 18.5 0.2 HH12 A:ARG21 4.2 28.7 0.3 H A:MET105 4.3 14.0 0.5 H A:MET105 4.4 15.2 0.2 H A:GLY104 4.4 19.5 0.3 H A:MET105 4.4 15.4 0.3 C A:ASN103 4.5 14.7 0.2 HB3 A:ARG21 4.5 24.8 0.3 O A:ARG21 4.5 19.2 0.3 NH1 A:ARG21 4.5 23.9 0.3 C A:ASN103 4.5 15.1 0.3 HB3 A:ARG21 4.6 20.1 0.3 C A:GLY104 4.6 15.3 0.3 C A:GLY104 4.6 14.9 0.2 O A:ASN103 4.6 13.4 0.3 HB3 A:ARG21 4.7 24.4 0.3 HH11 A:ARG21 4.7 28.7 0.3 HG22 A:VAL99 4.7 20.0 0.4 CD1 A:TYR23 4.7 12.4 0.3 C A:ASN103 4.8 14.4 0.2 O A:ASN103 4.8 15.2 0.2 C A:GLY104 4.8 13.2 0.5 CD2 A:TYR23 4.8 13.5 0.3 CE1 A:TYR23 4.8 11.9 0.3 HG22 A:VAL99 4.8 18.5 0.3 O A:ARG21 4.8 16.7 0.3 N A:MET105 4.8 12.6 0.3 N A:MET105 4.9 11.6 0.3 N A:MET105 4.9 12.8 0.5 O A:VAL99 4.9 15.5 0.4 O A:ARG21 4.9 17.3 0.3 C A:ASN103 4.9 13.1 0.3 O A:VAL99 4.9 17.6 0.3 CD1 A:TYR23 4.9 13.4 0.3 O A:GLY102 4.9 23.6 0.4 HD1 A:TYR23 5.0 14.9 0.3 O A:VAL99 5.0 18.5 0.3 O A:HOH308 5.0 22.0 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