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Sodium in PDB 5kdj: Zmpb Metallopeptidase From Clostridium Perfringens

Protein crystallography data

The structure of Zmpb Metallopeptidase From Clostridium Perfringens, PDB code: 5kdj was solved by I.Noach, E.Ficko-Blean, C.Stuart, A.B.Boraston, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.82 / 2.15
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 65.620, 95.800, 187.220, 90.00, 90.00, 90.00
R / Rfree (%) 19.1 / 22.9

Other elements in 5kdj:

The structure of Zmpb Metallopeptidase From Clostridium Perfringens also contains other interesting chemical elements:

Zinc (Zn) 2 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Zmpb Metallopeptidase From Clostridium Perfringens (pdb code 5kdj). 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 Zmpb Metallopeptidase From Clostridium Perfringens, PDB code: 5kdj:

Sodium binding site 1 out of 1 in 5kdj

Go back to Sodium Binding Sites List in 5kdj
Sodium binding site 1 out of 1 in the Zmpb Metallopeptidase From Clostridium Perfringens


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Zmpb Metallopeptidase From Clostridium Perfringens within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na1102

b:27.1
occ:1.00
N B:THR680 3.6 13.3 1.0
OG1 B:THR680 3.6 12.5 1.0
O B:HOH1554 3.7 35.2 1.0
CB B:TYR683 3.9 12.7 1.0
N B:TYR683 4.1 12.4 1.0
CG2 B:THR680 4.2 12.3 1.0
CA B:LYS679 4.2 15.2 1.0
CB B:THR680 4.3 12.6 1.0
O B:THR680 4.3 12.4 1.0
C B:LYS679 4.4 14.0 1.0
CA B:THR680 4.4 12.8 1.0
CD B:LYS679 4.4 16.9 1.0
CA B:TYR683 4.5 12.1 1.0
CB B:LYS679 4.6 15.8 1.0
C B:THR680 4.7 12.3 1.0
CG B:TYR683 4.8 13.6 1.0
CD1 B:TYR683 4.9 13.6 1.0
CB B:LYS682 5.0 14.0 1.0

Reference:

I.Noach, E.Ficko-Blean, B.Pluvinage, C.Stuart, M.L.Jenkins, D.Brochu, N.Buenbrazo, W.Wakarchuk, J.E.Burke, M.Gilbert, A.B.Boraston. Recognition of Protein-Linked Glycans As A Determinant of Peptidase Activity. Proc. Natl. Acad. Sci. V. 114 E679 2017U.S.A..
ISSN: ESSN 1091-6490
PubMed: 28096352
DOI: 10.1073/PNAS.1615141114
Page generated: Tue Dec 15 11:10:10 2020

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