Sodium in PDB 6nz8: Structure of Carbamylated Apo Oxa-231 Carbapenemase

The structure of Structure of Carbamylated Apo Oxa-231 Carbapenemase, PDB code: 6nz8 was solved by D.C.Favaro, E.E.Llontop, F.N.Vasconcelos, V.U.Antunes, S.C.Farah, N.Lincopan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.77 / 1.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	39.786, 54.786, 96.243, 90.00, 90.00, 90.00
R / Rfree (%)	16.7 / 19.4

The structure of Structure of Carbamylated Apo Oxa-231 Carbapenemase also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

The binding sites of Sodium atom in the Structure of Carbamylated Apo Oxa-231 Carbapenemase (pdb code 6nz8). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Structure of Carbamylated Apo Oxa-231 Carbapenemase, PDB code: 6nz8:

Sodium binding site 1 out of 1 in the Structure of Carbamylated Apo Oxa-231 Carbapenemase


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Structure of Carbamylated Apo Oxa-231 Carbapenemase within 5.0Å range: probe atom residue distance (Å) B Occ A:Na301 b:20.7 occ:1.00 HD22 A:ASN87 2.0 16.8 1.0 HD2 A:PHE83 2.8 15.6 1.0 OQ1 A:KCX84 2.8 16.6 1.0 HB3 A:TYR133 2.8 15.5 1.0 HG3 A:KCX84 2.9 17.0 1.0 ND2 A:ASN87 2.9 14.0 1.0 CE2 A:TRP167 3.2 12.9 1.0 NE1 A:TRP167 3.2 14.6 1.0 HB2 A:ASN87 3.3 16.3 1.0 HG2 A:KCX84 3.3 17.0 1.0 HE1 A:TRP167 3.3 17.5 1.0 CZ2 A:TRP167 3.3 14.0 1.0 HD21 A:ASN87 3.3 16.8 1.0 HZ2 A:TRP167 3.4 16.8 1.0 CG A:KCX84 3.5 14.2 1.0 CB A:TYR133 3.6 12.9 1.0 HB3 A:ASN87 3.6 16.3 1.0 CD2 A:PHE83 3.7 13.0 1.0 HB3 A:PHE83 3.7 13.6 1.0 HB2 A:TYR133 3.7 15.5 1.0 CX A:KCX84 3.7 17.1 1.0 CA A:KCX84 3.7 12.9 1.0 N A:KCX84 3.7 12.4 1.0 CB A:ASN87 3.8 13.6 1.0 CD2 A:TRP167 3.8 12.8 1.0 CG A:ASN87 3.8 13.6 1.0 HD2 A:TYR133 3.9 18.4 1.0 CD1 A:TRP167 3.9 14.1 1.0 CH2 A:TRP167 4.0 14.8 1.0 C A:PHE83 4.1 11.5 1.0 CB A:KCX84 4.2 14.3 1.0 CG A:TRP167 4.2 13.8 1.0 CG A:TYR133 4.2 13.4 1.0 O A:PHE83 4.3 12.7 1.0 CD2 A:TYR133 4.3 15.3 1.0 HE2 A:PHE83 4.3 16.0 1.0 HE2 A:KCX84 4.3 20.0 1.0 OQ2 A:KCX84 4.3 19.5 1.0 HD1 A:TRP167 4.4 16.9 1.0 CB A:PHE83 4.4 11.3 1.0 CE3 A:TRP167 4.4 13.7 1.0 CE2 A:PHE83 4.5 13.3 1.0 CG A:PHE83 4.5 11.6 1.0 HH2 A:TRP167 4.5 17.7 1.0 CZ3 A:TRP167 4.5 14.9 1.0 HB2 A:KCX84 4.6 17.2 1.0 NZ A:KCX84 4.6 17.2 1.0 CD A:KCX84 4.7 16.6 1.0 HA A:SER81 4.7 16.0 1.0 CE A:KCX84 4.7 16.7 1.0 HB3 A:KCX84 4.8 17.2 1.0 O A:TYR133 4.8 13.0 1.0 CA A:PHE83 4.8 12.4 1.0 CA A:TYR133 4.8 12.6 1.0 H A:ASN87 4.9 16.3 1.0 C A:TYR133 4.9 12.8 1.0 OD1 A:ASN87 5.0 15.8 1.0

D.C.Favaro, E.E.Llontop, F.N.Vasconcelos, V.U.Antunes, S.C.Farah, N.Lincopan. Structure of Carbamylated Apo Oxa-231 Carbapenemase To Be Published.