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Sodium in PDB 6kl8: Crystal Structure of Piptidyl T-Rna Hydrolase From Acinetobacter Baumannii with Bound Nacl at the Substrate Binding Site

Enzymatic activity of Crystal Structure of Piptidyl T-Rna Hydrolase From Acinetobacter Baumannii with Bound Nacl at the Substrate Binding Site

All present enzymatic activity of Crystal Structure of Piptidyl T-Rna Hydrolase From Acinetobacter Baumannii with Bound Nacl at the Substrate Binding Site:
3.1.1.29;

Protein crystallography data

The structure of Crystal Structure of Piptidyl T-Rna Hydrolase From Acinetobacter Baumannii with Bound Nacl at the Substrate Binding Site, PDB code: 6kl8 was solved by V.Viswanathan, P.Sharma, P.K.Singh, S.Sharma, T.P.Singh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 31.01 / 1.94
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 33.961, 66.099, 75.825, 90.00, 90.00, 90.00
R / Rfree (%) 12.7 / 16.4

Other elements in 6kl8:

The structure of Crystal Structure of Piptidyl T-Rna Hydrolase From Acinetobacter Baumannii with Bound Nacl at the Substrate Binding Site also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of Piptidyl T-Rna Hydrolase From Acinetobacter Baumannii with Bound Nacl at the Substrate Binding Site (pdb code 6kl8). 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 Crystal Structure of Piptidyl T-Rna Hydrolase From Acinetobacter Baumannii with Bound Nacl at the Substrate Binding Site, PDB code: 6kl8:

Sodium binding site 1 out of 1 in 6kl8

Go back to Sodium Binding Sites List in 6kl8
Sodium binding site 1 out of 1 in the Crystal Structure of Piptidyl T-Rna Hydrolase From Acinetobacter Baumannii with Bound Nacl at the Substrate Binding Site


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of Piptidyl T-Rna Hydrolase From Acinetobacter Baumannii with Bound Nacl at the Substrate Binding Site within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na202

b:21.5
occ:0.85
N A:ASN70 3.0 11.1 1.0
CL A:CL201 3.1 19.3 0.8
N A:MET69 3.4 9.2 1.0
CG A:ASN70 3.4 19.9 1.0
OD1 A:ASN70 3.5 25.4 1.0
CB A:ASN70 3.6 15.1 1.0
CB A:MET69 3.7 8.9 1.0
CA A:ASN70 3.8 12.3 1.0
CA A:MET69 3.9 9.2 1.0
ND2 A:ASN116 3.9 21.3 1.0
C A:MET69 3.9 9.7 1.0
ND2 A:ASN70 3.9 25.7 1.0
OD1 A:ASN12 3.9 8.3 1.0
CB A:TYR68 4.0 13.2 1.0
C A:TYR68 4.1 9.3 1.0
CA A:TYR68 4.6 10.9 1.0
O A:TYR68 4.8 8.6 1.0
ND2 A:ASN12 4.8 8.0 1.0
CG A:ASN12 4.8 8.1 1.0
CG A:MET69 4.9 8.9 1.0
CG A:ASN116 4.9 20.2 1.0
C A:ASN70 4.9 10.8 1.0

Reference:

V.Viswanathan, P.Sharma, P.K.Singh, S.Sharma, T.P.Singh. Crystal Structure of Piptidyl T-Rna Hydrolase From Acinetobacter Baumannii with Bound Nacl at the Substrate Binding Site To Be Published.
Page generated: Tue Oct 8 11:33:00 2024

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