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Calcium in PDB 6nff: Structure of X-Prolyl Dipeptidyl Aminopeptidase From Lactobacillus Helveticus

Enzymatic activity of Structure of X-Prolyl Dipeptidyl Aminopeptidase From Lactobacillus Helveticus

All present enzymatic activity of Structure of X-Prolyl Dipeptidyl Aminopeptidase From Lactobacillus Helveticus:
3.4.14.11;

Protein crystallography data

The structure of Structure of X-Prolyl Dipeptidyl Aminopeptidase From Lactobacillus Helveticus, PDB code: 6nff was solved by D.H.Juers, N.J.Bratt, D.D.Ojennus, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.30 / 2.00
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 154.630, 154.630, 106.594, 90.00, 90.00, 90.00
R / Rfree (%) 23.6 / 27.3

Calcium Binding Sites:

The binding sites of Calcium atom in the Structure of X-Prolyl Dipeptidyl Aminopeptidase From Lactobacillus Helveticus (pdb code 6nff). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Structure of X-Prolyl Dipeptidyl Aminopeptidase From Lactobacillus Helveticus, PDB code: 6nff:

Calcium binding site 1 out of 1 in 6nff

Go back to Calcium Binding Sites List in 6nff
Calcium binding site 1 out of 1 in the Structure of X-Prolyl Dipeptidyl Aminopeptidase From Lactobacillus Helveticus


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of X-Prolyl Dipeptidyl Aminopeptidase From Lactobacillus Helveticus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca801

b:34.2
occ:0.99
O A:LYS200 2.3 29.1 1.0
O A:HOH1137 2.3 30.4 1.0
OD1 A:ASP196 2.3 36.1 1.0
OD1 A:ASP202 2.4 31.3 1.0
OD1 A:ASP194 2.4 34.9 1.0
OD1 A:ASP198 2.5 31.2 1.0
CG A:ASP198 3.2 35.2 1.0
CG A:ASP196 3.4 38.0 1.0
CG A:ASP194 3.4 36.9 1.0
C A:LYS200 3.4 37.7 1.0
CG A:ASP202 3.6 33.5 1.0
OD2 A:ASP198 3.7 32.0 1.0
CA A:ASP194 3.7 32.2 1.0
OD2 A:ASP196 3.8 35.9 1.0
CB A:ASP194 3.9 29.0 1.0
N A:ASP202 4.0 30.1 1.0
C A:SER201 4.0 33.2 1.0
N A:LYS200 4.1 37.3 1.0
O A:SER201 4.1 33.9 1.0
CA A:LYS200 4.2 34.2 1.0
CA A:ASP202 4.2 29.8 1.0
C A:ASP194 4.2 35.6 1.0
N A:ASP198 4.3 32.5 1.0
O A:LEU193 4.3 30.1 1.0
CB A:ASP198 4.3 32.0 1.0
N A:ASP196 4.4 32.3 1.0
OD2 A:ASP194 4.4 38.8 1.0
OD2 A:ASP202 4.4 31.5 1.0
N A:SER201 4.5 32.7 1.0
CB A:LYS200 4.5 40.1 1.0
CB A:ASP202 4.5 34.4 1.0
N A:THR195 4.6 30.0 1.0
N A:HIS197 4.6 35.3 1.0
CB A:ASP196 4.7 31.1 1.0
CA A:SER201 4.7 35.0 1.0
CA A:ASP198 4.7 35.2 1.0
O A:ASP194 4.8 32.6 1.0
CB A:ASP311 4.8 27.1 1.0
C A:ASP196 4.8 36.6 1.0
CA A:ASP196 4.8 35.0 1.0
N A:ASP194 4.9 29.3 1.0
N A:GLY199 4.9 35.1 1.0
C A:ASP198 5.0 34.5 1.0

Reference:

D.D.Ojennus, N.J.Bratt, K.L.Jones, D.H.Juers. Structural Characterization of A Prolyl Aminodipeptidase (Pepx) From Lactobacillus Helveticus. Acta Crystallogr.,Sect.F V. 75 625 2019.
ISSN: ESSN 2053-230X
PubMed: 31584010
DOI: 10.1107/S2053230X19011774
Page generated: Tue Jul 16 11:42:07 2024

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