Chlorine in PDB 4o0c: High Resolution Crystal Structure of Uncleaved Human L-Asparaginase Protein

All present enzymatic activity of High Resolution Crystal Structure of Uncleaved Human L-Asparaginase Protein:
3.4.19.5; 3.5.1.1;

The structure of High Resolution Crystal Structure of Uncleaved Human L-Asparaginase Protein, PDB code: 4o0c was solved by J.Nomme, A.Lavie, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.04 / 1.50
Space group	P 65
Cell size a, b, c (Å), α, β, γ (°)	59.213, 59.213, 297.793, 90.00, 90.00, 120.00
R / Rfree (%)	15.2 / 20.5

The structure of High Resolution Crystal Structure of Uncleaved Human L-Asparaginase Protein also contains other interesting chemical elements:

Sodium

(Na)

5 atoms

The binding sites of Chlorine atom in the High Resolution Crystal Structure of Uncleaved Human L-Asparaginase Protein (pdb code 4o0c). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the High Resolution Crystal Structure of Uncleaved Human L-Asparaginase Protein, PDB code: 4o0c:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the High Resolution Crystal Structure of Uncleaved Human L-Asparaginase Protein


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of High Resolution Crystal Structure of Uncleaved Human L-Asparaginase Protein within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl404 b:25.9 occ:1.00 O A:HOH510 3.1 16.1 1.0 N A:ASN2 3.3 16.1 1.0 O A:HOH586 3.3 24.8 1.0 CG A:ASN2 3.5 15.2 1.0 OD1 A:ASN2 3.6 18.4 1.0 CE A:MET1 3.6 16.4 1.0 CB A:ASN2 3.8 15.2 1.0 CA A:MET1 4.0 15.1 1.0 ND2 A:ASN2 4.0 18.4 1.0 CA A:ASN2 4.1 15.8 1.0 C A:MET1 4.1 16.2 1.0 SD A:MET1 4.3 20.5 1.0 CB A:MET1 4.5 15.5 1.0 O A:ASN2 4.6 15.8 1.0 NZ A:LYS289 4.7 19.9 1.0 O A:HIS0 4.8 20.9 1.0 O A:HOH604 4.8 19.8 1.0 C A:ASN2 4.9 14.2 1.0

Chlorine binding site 2 out of 2 in the High Resolution Crystal Structure of Uncleaved Human L-Asparaginase Protein


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of High Resolution Crystal Structure of Uncleaved Human L-Asparaginase Protein within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl405 b:25.2 occ:1.00 N B:ASN2 3.0 13.6 1.0 O B:HOH572 3.1 17.9 1.0 CE B:MET1 3.7 21.7 1.0 CB B:ASN2 3.7 16.1 1.0 CA B:MET1 3.8 16.3 1.0 C B:MET1 3.9 15.1 1.0 SD B:MET1 3.9 20.1 1.0 CA B:ASN2 4.0 15.2 1.0 CG B:ASN2 4.0 15.1 1.0 OD1 B:ASN2 4.1 17.2 1.0 CB B:MET1 4.2 15.2 1.0 O B:ASN2 4.7 20.7 1.0 CG B:MET1 4.8 18.4 1.0 ND2 B:ASN2 4.8 19.1 1.0 C B:ASN2 4.9 13.6 1.0 N B:MET1 5.0 16.3 1.0 O B:HIS0 5.0 18.1 1.0

J.Nomme, Y.Su, A.Lavie. Elucidation of the Specific Function of the Conserved Threonine Triad Responsible For Human L-Asparaginase Autocleavage and Substrate Hydrolysis. J.Mol.Biol. V. 426 2471 2014.
ISSN: ISSN 0022-2836
PubMed: 24768817
DOI: 10.1016/J.JMB.2014.04.016