Chlorine in PDB 3i7w: High Pressure Structure of Wild-Type Rnase A (0.67 Gpa)

All present enzymatic activity of High Pressure Structure of Wild-Type Rnase A (0.67 Gpa):
3.1.27.5;

The structure of High Pressure Structure of Wild-Type Rnase A (0.67 Gpa), PDB code: 3i7w was solved by K.Lewinski, K.Kurpiewska, K.Dziubek, A.Katrusiak, J.Font, M.Ribo, M.Vilanova, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.35
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	63.552, 63.552, 63.300, 90.00, 90.00, 120.00
R / Rfree (%)	25.2 / 29.5

The binding sites of Chlorine atom in the High Pressure Structure of Wild-Type Rnase A (0.67 Gpa) (pdb code 3i7w). 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 Pressure Structure of Wild-Type Rnase A (0.67 Gpa), PDB code: 3i7w:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the High Pressure Structure of Wild-Type Rnase A (0.67 Gpa)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of High Pressure Structure of Wild-Type Rnase A (0.67 Gpa) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl125 b:22.0 occ:1.00 N A:THR78 3.3 11.3 1.0 OG1 A:THR78 3.4 13.7 1.0 CG2 A:THR78 3.7 11.7 1.0 CA A:SER77 3.9 13.2 1.0 CB A:SER77 3.9 12.5 1.0 CB A:THR78 4.0 11.7 1.0 C A:SER77 4.1 13.3 1.0 CA A:THR78 4.2 12.3 1.0 NE2 A:HIS105 4.7 10.1 1.0 O A:THR78 4.9 14.9 1.0 OG A:SER77 5.0 18.4 1.0

Chlorine binding site 2 out of 2 in the High Pressure Structure of Wild-Type Rnase A (0.67 Gpa)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of High Pressure Structure of Wild-Type Rnase A (0.67 Gpa) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl126 b:20.0 occ:1.00 N A:THR45 3.0 9.9 1.0 CB A:THR45 3.6 12.1 1.0 CE1 A:HIS12 3.6 9.9 1.0 CA A:ASN44 3.7 8.0 1.0 OG1 A:THR45 3.7 12.2 1.0 C A:ASN44 3.7 8.6 1.0 CD1 A:PHE120 3.7 17.7 1.0 CA A:THR45 3.9 9.1 1.0 ND1 A:HIS12 4.1 11.4 1.0 CB A:PHE120 4.1 19.3 1.0 CG A:PHE120 4.1 18.0 1.0 N A:ASN44 4.4 8.7 1.0 O A:PHE120 4.4 21.6 1.0 OD1 A:ASN44 4.4 12.8 1.0 CE1 A:PHE120 4.5 19.1 1.0 O A:THR45 4.6 9.6 1.0 NE2 A:HIS12 4.6 8.7 1.0 O A:VAL43 4.7 6.0 1.0 C A:THR45 4.8 9.5 1.0 CB A:ASN44 4.8 9.4 1.0 C A:VAL43 4.8 9.1 1.0 O A:ASN44 4.8 8.2 1.0 CG A:ASN44 4.9 9.7 1.0 CG1 A:VAL43 4.9 5.3 1.0 CG2 A:THR45 5.0 13.1 1.0

K.Kurpiewska, K.Dziubek, A.Katrusiak, J.Font, M.Ribo, M.Vilanova, K.Lewinski. Structural Investigation of Ribonuclease A Conformational Preferences Using High Pressure Protein Crystallography Chem.Phys. V. 468 53 2016.
ISSN: ISSN 0301-0104
DOI: 10.1016/J.CHEMPHYS.2016.01.010