Chlorine in PDB 3dh5: Crystal Structure of Bovine Pancreatic Ribonuclease A (Wild-Type)

All present enzymatic activity of Crystal Structure of Bovine Pancreatic Ribonuclease A (Wild-Type):
3.1.27.5;

The structure of Crystal Structure of Bovine Pancreatic Ribonuclease A (Wild-Type), PDB code: 3dh5 was solved by K.Kurpiewska, J.Font, M.Ribo, M.Vilanova, K.Lewinski, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.60
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	64.129, 64.129, 63.803, 90.00, 90.00, 120.00
R / Rfree (%)	17.5 / 21.5

The binding sites of Chlorine atom in the Crystal Structure of Bovine Pancreatic Ribonuclease A (Wild-Type) (pdb code 3dh5). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Crystal Structure of Bovine Pancreatic Ribonuclease A (Wild-Type), PDB code: 3dh5:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Crystal Structure of Bovine Pancreatic Ribonuclease A (Wild-Type)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Bovine Pancreatic Ribonuclease A (Wild-Type) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl125 b:10.3 occ:1.00 OG1 A:THR3 3.1 7.0 1.0 O A:HOH1132 3.2 10.8 1.0 O A:HOH1008 3.2 9.5 1.0 CB A:THR3 4.0 5.9 1.0 CG2 A:THR3 4.1 10.7 1.0 N A:ALA6 4.2 4.3 1.0 CB A:ALA5 4.2 5.1 1.0 CB A:ALA6 4.2 6.6 1.0 O A:HOH1145 4.3 13.4 1.0 CA A:ALA6 4.7 4.2 1.0 O A:HOH1099 4.9 12.5 1.0 C A:ALA5 4.9 6.6 1.0 O A:HOH1032 5.0 11.5 1.0

Chlorine binding site 2 out of 4 in the Crystal Structure of Bovine Pancreatic Ribonuclease A (Wild-Type)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Bovine Pancreatic Ribonuclease A (Wild-Type) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl126 b:22.3 occ:1.00 O A:HOH1133 2.9 28.9 1.0 O A:HOH1012 2.9 7.8 1.0 O A:HOH1173 3.0 37.0 1.0 CB A:SER15 3.7 8.2 1.0 CB A:SER50 3.8 8.0 1.0 CA A:SER50 3.9 6.1 1.0 O A:SER15 4.3 21.2 1.0 OG A:SER15 4.3 7.2 1.0 N A:SER50 4.7 7.8 1.0 O A:HOH1010 4.8 10.0 1.0 CA A:SER15 4.9 8.3 1.0 C A:SER15 4.9 17.8 1.0 O A:HOH1154 4.9 32.7 1.0 O A:HOH1111 5.0 26.8 1.0 O A:HOH1140 5.0 20.2 1.0

Chlorine binding site 3 out of 4 in the Crystal Structure of Bovine Pancreatic Ribonuclease A (Wild-Type)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of Bovine Pancreatic Ribonuclease A (Wild-Type) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl127 b:35.5 occ:1.00 O A:HOH1019 2.8 8.9 1.0 CG A:GLU2 3.9 9.7 1.0 CB A:ALA6 3.9 6.6 1.0 OE2 A:GLU2 4.2 11.5 1.0 CD A:GLU2 4.5 8.3 1.0 O A:HOH1060 4.6 15.5 1.0 CB A:GLU2 4.6 10.7 1.0 CA A:GLU2 4.6 8.7 1.0 O A:HOH1020 4.8 10.0 1.0

Chlorine binding site 4 out of 4 in the Crystal Structure of Bovine Pancreatic Ribonuclease A (Wild-Type)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Crystal Structure of Bovine Pancreatic Ribonuclease A (Wild-Type) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl128 b:11.4 occ:1.00 O A:HOH1184 2.9 32.9 1.0 O A:HOH1088 3.2 33.5 1.0 N A:THR45 3.2 5.7 1.0 O A:HOH1137 3.4 25.6 1.0 CE1 A:HIS12 3.5 6.7 1.0 O A:HOH1118 3.6 28.2 1.0 CA A:ASN44 3.7 7.1 1.0 OG1 A:THR45 3.7 9.1 1.0 CD2 A:PHE120 3.8 9.7 1.0 C A:ASN44 3.9 5.8 1.0 CB A:THR45 4.0 7.6 1.0 CA A:THR45 4.2 3.3 1.0 ND1 A:HIS12 4.2 5.7 1.0 CB A:PHE120 4.2 7.1 1.0 O A:VAL43 4.3 8.1 1.0 CG A:PHE120 4.3 6.5 1.0 N A:ASN44 4.4 6.9 1.0 NE2 A:HIS12 4.4 8.2 1.0 OD1 A:ASN44 4.4 11.1 1.0 O A:PHE120 4.5 10.9 1.0 NZ A:LYS41 4.5 20.9 1.0 O A:HOH1182 4.6 33.1 1.0 C A:VAL43 4.6 7.8 1.0 CE2 A:PHE120 4.6 9.6 1.0 CG1 A:VAL43 4.7 14.5 1.0 CB A:ASN44 4.8 8.7 1.0 CG A:ASN44 4.8 8.6 1.0 O A:THR45 4.9 8.3 1.0

K.Kurpiewska, J.Font, M.Ribo, M.Vilanova, K.Lewinski. X-Ray Crystallographic Studies of Rnase A Variants Engineered at the Most Destabilizing Positions of the Main Hydrophobic Core: Further Insight Into Protein Stability Proteins V. 77 658 2009.
ISSN: ISSN 0887-3585
PubMed: 19544568
DOI: 10.1002/PROT.22480