Chlorine in PDB 5kxl: Hen Egg White Lysozyme at 100K, Data Set 2

All present enzymatic activity of Hen Egg White Lysozyme at 100K, Data Set 2:
3.2.1.17;

The structure of Hen Egg White Lysozyme at 100K, Data Set 2, PDB code: 5kxl was solved by S.Russi, A.Gonzalez, L.R.Kenner, D.A.Keedy, J.S.Fraser, H.Van Den Bedem, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.66 / 1.20
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	77.312, 77.312, 37.213, 90.00, 90.00, 90.00
R / Rfree (%)	15 / 16.4

The structure of Hen Egg White Lysozyme at 100K, Data Set 2 also contains other interesting chemical elements:

Sodium

(Na)

2 atoms

The binding sites of Chlorine atom in the Hen Egg White Lysozyme at 100K, Data Set 2 (pdb code 5kxl). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Hen Egg White Lysozyme at 100K, Data Set 2, PDB code: 5kxl:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Hen Egg White Lysozyme at 100K, Data Set 2


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Hen Egg White Lysozyme at 100K, Data Set 2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl201 b:11.5 occ:1.00 O A:THR69 3.0 12.2 0.2 O A:HOH428 3.1 18.8 1.0 O A:HOH354 3.1 8.9 1.0 O A:HOH381 3.2 15.6 1.0 N A:THR69 3.3 9.0 0.4 O A:HOH312 3.3 21.4 1.0 N A:THR69 3.3 9.5 0.4 N A:THR69 3.3 11.5 0.2 O A:THR69 3.4 8.6 0.4 OG A:SER72 3.4 12.6 0.6 O A:THR69 3.5 10.5 0.4 OG A:SER72 3.5 12.1 0.4 N A:ARG68 3.5 9.6 0.4 C A:GLY67 3.6 10.2 1.0 N A:ARG68 3.6 9.6 0.4 CA A:GLY67 3.6 9.8 1.0 N A:ARG68 3.6 10.6 0.2 OD1 A:ASN65 3.6 7.8 0.5 C A:THR69 3.7 12.2 0.2 N A:GLY67 3.7 8.9 1.0 C A:THR69 3.7 10.3 0.4 C A:THR69 3.8 9.9 0.4 OD1 A:ASN65 3.8 8.5 0.1 O A:HOH351 3.9 11.6 1.0 CA A:THR69 3.9 9.5 0.4 CA A:THR69 3.9 10.0 0.4 CA A:THR69 4.0 11.9 0.2 OD1 A:ASN65 4.0 9.7 0.4 O A:GLY67 4.2 12.1 1.0 CB A:THR69 4.2 10.3 0.4 CB A:THR69 4.2 9.1 0.4 OD1 A:ASP66 4.2 9.1 0.1 C A:ARG68 4.3 9.8 0.4 OD1 A:ASP66 4.3 6.7 0.5 C A:ARG68 4.3 9.3 0.4 CA A:ARG68 4.3 9.8 0.4 C A:ARG68 4.3 11.4 0.2 CB A:THR69 4.4 11.8 0.2 OD1 A:ASP66 4.4 8.7 0.4 CA A:ARG68 4.4 9.6 0.4 CA A:ARG68 4.4 11.2 0.2 N A:PRO70 4.5 11.4 0.4 O A:HOH440 4.6 34.1 1.0 N A:PRO70 4.6 11.2 0.4 NA A:NA204 4.6 9.8 1.0 CB A:SER72 4.7 12.6 0.6 N A:PRO70 4.7 12.5 0.2 C A:ASP66 4.8 8.3 0.5 CB A:SER72 4.8 12.1 0.4 C A:ASP66 4.8 9.0 0.1 OG1 A:THR69 4.8 8.2 0.4 O A:HOH367 4.8 13.8 0.5 CG A:ASN65 4.8 8.5 0.5 C A:ASP66 4.8 8.4 0.4 CG A:ASN65 4.9 8.6 0.1 N A:ASP66 4.9 6.9 0.5 N A:ASP66 4.9 8.6 0.1 OG1 A:THR69 4.9 9.7 0.4 N A:ASP66 4.9 7.4 0.4 CA A:PRO70 5.0 12.2 0.4 OG1 A:THR69 5.0 11.3 0.2

Chlorine binding site 2 out of 3 in the Hen Egg White Lysozyme at 100K, Data Set 2


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Hen Egg White Lysozyme at 100K, Data Set 2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl202 b:11.0 occ:1.00 OH A:TYR23 3.0 8.2 0.7 OH A:TYR23 3.0 8.2 0.3 CZ A:TYR23 3.7 7.5 0.7 CZ A:TYR23 3.7 8.1 0.3 CE2 A:TYR23 3.7 8.0 0.3 CE2 A:TYR23 3.7 7.1 0.7 CA A:GLY104 4.2 8.4 1.0 O A:ARG21 4.5 10.9 1.0 N A:GLY104 4.8 8.3 1.0 CE1 A:TYR23 4.8 8.0 0.3 CE1 A:TYR23 4.9 7.5 0.7 CD2 A:TYR23 4.9 8.0 0.3 CD2 A:TYR23 4.9 7.4 0.7

Chlorine binding site 3 out of 3 in the Hen Egg White Lysozyme at 100K, Data Set 2


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Hen Egg White Lysozyme at 100K, Data Set 2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl203 b:16.8 occ:1.00 OG A:SER24 3.0 13.2 0.7 N A:GLY26 3.1 8.2 1.0 OG A:SER24 3.3 7.9 0.3 CA A:GLY26 3.5 8.4 1.0 CD1 A:ILE124 3.5 14.5 0.5 CB A:SER24 3.5 11.9 0.7 CB A:SER24 3.6 8.4 0.3 CA A:GLN121 3.6 12.8 0.5 CA A:GLN121 3.9 16.2 0.5 N A:GLN121 4.0 13.3 0.5 CB A:GLN121 4.0 15.3 0.5 N A:LEU25 4.1 8.7 0.3 O A:VAL120 4.1 15.6 0.5 CG2 A:VAL120 4.1 17.5 0.5 CG1 A:ILE124 4.1 13.4 0.5 N A:LEU25 4.1 8.9 0.7 N A:GLN121 4.2 13.2 0.5 CG A:GLN121 4.2 17.5 0.5 C A:VAL120 4.2 14.4 0.5 O A:VAL120 4.3 9.5 0.5 C A:LEU25 4.3 7.8 0.7 C A:LEU25 4.3 8.0 0.3 C A:SER24 4.3 9.0 0.7 C A:VAL120 4.3 10.2 0.5 CD1 A:ILE124 4.3 13.9 0.5 CG A:GLN121 4.4 22.0 0.5 NE2 A:GLN121 4.4 25.1 0.5 C A:SER24 4.4 8.0 0.3 CB A:GLN121 4.5 19.3 0.5 CA A:SER24 4.5 10.0 0.7 CD A:GLN121 4.5 24.1 0.5 CG2 A:VAL120 4.5 12.1 0.5 C A:GLY26 4.5 7.7 1.0 N A:ASN27 4.6 7.6 0.4 CG1 A:ILE124 4.6 13.2 0.5 CA A:SER24 4.6 8.2 0.3 CA A:LEU25 4.6 8.9 0.7 CA A:LEU25 4.7 8.5 0.3 N A:ASN27 4.7 7.5 0.4 N A:ASN27 4.7 7.7 0.2 O A:SER24 4.7 9.1 0.7 C A:GLN121 4.8 10.0 0.5 O A:HOH374 4.8 11.5 0.4 CB A:VAL120 4.9 16.6 0.5 CB A:LEU25 4.9 9.2 0.7 O A:SER24 5.0 8.2 0.3 C A:GLN121 5.0 16.2 0.5

S.Russi, A.Gonzalez, L.R.Kenner, D.A.Keedy, J.S.Fraser, H.Van Den Bedem. Conformational Variation of Proteins at Room Temperature Is Not Dominated By Radiation Damage. J Synchrotron Radiat V. 24 73 2017.
ISSN: ESSN 1600-5775
PubMed: 28009548
DOI: 10.1107/S1600577516017343