Chlorine in PDB 5kxn: Hen Egg White Lysozyme at 100K, Data Set 4

All present enzymatic activity of Hen Egg White Lysozyme at 100K, Data Set 4:
3.2.1.17;

The structure of Hen Egg White Lysozyme at 100K, Data Set 4, PDB code: 5kxn 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 (°)	77.311, 77.311, 37.212, 90.00, 90.00, 90.00
R / Rfree (%)	15.9 / 17.8

The structure of Hen Egg White Lysozyme at 100K, Data Set 4 also contains other interesting chemical elements:

Sodium

(Na)

1 atom

The binding sites of Chlorine atom in the Hen Egg White Lysozyme at 100K, Data Set 4 (pdb code 5kxn). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Hen Egg White Lysozyme at 100K, Data Set 4, PDB code: 5kxn:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Hen Egg White Lysozyme at 100K, Data Set 4


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 4 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl201 b:20.8 occ:1.00 OH A:TYR23 3.0 11.5 0.3 OH A:TYR23 3.1 11.3 0.2 OH A:TYR23 3.2 9.4 0.5 O A:HOH362 3.6 13.0 1.0 CE2 A:TYR23 3.8 9.8 0.3 CZ A:TYR23 3.8 9.7 0.3 CE2 A:TYR23 3.8 9.5 0.5 CZ A:TYR23 3.8 10.4 0.2 CE2 A:TYR23 3.8 10.4 0.2 CZ A:TYR23 3.8 9.2 0.5 CA A:GLY104 3.9 10.0 1.0 N A:GLY104 4.4 9.9 1.0 O A:ARG21 4.6 12.3 1.0 CG A:ARG21 4.9 16.4 0.3 O A:HOH333 5.0 14.3 1.0 C A:ASN103 5.0 10.7 0.5 C A:ASN103 5.0 9.6 0.6 CE1 A:TYR23 5.0 9.2 0.3

Chlorine binding site 2 out of 2 in the Hen Egg White Lysozyme at 100K, Data Set 4


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 4 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl202 b:20.2 occ:1.00 OG A:SER24 3.0 13.9 0.3 OG A:SER24 3.0 14.1 0.5 N A:GLY26 3.1 10.1 1.0 OG A:SER24 3.3 8.9 0.2 CB A:SER24 3.4 12.7 0.3 CA A:GLY26 3.5 10.4 1.0 CB A:SER24 3.5 13.1 0.5 CB A:SER24 3.6 9.6 0.2 CA A:GLN121 3.6 11.1 0.5 CG2 A:VAL120 3.7 15.3 0.3 O A:VAL120 4.0 15.6 0.3 N A:GLN121 4.0 10.1 0.5 CB A:GLN121 4.1 14.4 0.5 N A:LEU25 4.1 11.0 0.3 CD1 A:ILE124 4.1 19.8 0.3 N A:LEU25 4.1 9.6 0.2 N A:LEU25 4.1 11.1 0.5 CD1 A:ILE124 4.1 15.9 0.2 CA A:GLN121 4.2 21.1 0.5 C A:VAL120 4.2 16.7 0.3 NE2 A:GLN121 4.2 24.8 0.5 C A:SER24 4.2 11.4 0.5 O A:VAL120 4.2 10.3 0.2 C A:VAL120 4.2 10.4 0.2 CD1 A:ILE124 4.2 18.7 0.4 CG A:GLN121 4.3 19.0 0.5 C A:LEU25 4.3 9.2 0.5 C A:LEU25 4.3 9.6 0.2 N A:GLN121 4.3 20.2 0.5 C A:LEU25 4.3 9.8 0.3 C A:SER24 4.3 9.4 0.2 C A:SER24 4.3 11.1 0.3 CG2 A:VAL120 4.4 13.4 0.4 CD A:GLN121 4.4 23.2 0.5 O A:VAL120 4.4 12.7 0.4 C A:VAL120 4.4 11.9 0.4 CG1 A:ILE124 4.4 18.6 0.3 CA A:SER24 4.5 11.8 0.3 CA A:SER24 4.5 12.5 0.5 CG1 A:ILE124 4.5 17.5 0.4 C A:GLY26 4.5 9.4 1.0 CB A:VAL120 4.5 14.4 0.3 CA A:SER24 4.6 10.0 0.2 CG2 A:VAL120 4.6 12.2 0.2 CA A:LEU25 4.6 10.3 0.5 CA A:LEU25 4.6 10.1 0.2 N A:ASN27 4.6 9.1 0.3 O A:SER24 4.6 11.5 0.5 N A:ASN27 4.6 9.1 0.4 CA A:LEU25 4.6 11.1 0.3 N A:ASN27 4.6 9.3 0.3 CG2 A:ILE124 4.7 13.5 0.2 CG1 A:ILE124 4.8 15.6 0.2 O A:SER24 4.8 9.4 0.2 C A:GLN121 4.8 9.9 0.5 O A:HOH377 4.8 13.2 0.5 O A:SER24 4.9 11.4 0.3 CB A:GLN121 4.9 23.7 0.5 CB A:LEU25 4.9 10.3 0.5 CB A:LEU25 4.9 10.9 0.2 CG A:GLN121 5.0 26.5 0.5 CB A:LEU25 5.0 12.0 0.3

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