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Zinc in PDB 8bjc: Full Length Structure of the Apo-State Lpmip.

Enzymatic activity of Full Length Structure of the Apo-State Lpmip.

All present enzymatic activity of Full Length Structure of the Apo-State Lpmip.:
5.2.1.8;

Protein crystallography data

The structure of Full Length Structure of the Apo-State Lpmip., PDB code: 8bjc was solved by J.J.Whittaker, A.Guskov, B.Goretzki, U.A.Hellmich, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 62.24 / 1.71
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 77.773, 77.773, 103.789, 90, 90, 90
R / Rfree (%) 23.9 / 28.8

Zinc Binding Sites:

The binding sites of Zinc atom in the Full Length Structure of the Apo-State Lpmip. (pdb code 8bjc). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Full Length Structure of the Apo-State Lpmip., PDB code: 8bjc:

Zinc binding site 1 out of 1 in 8bjc

Go back to Zinc Binding Sites List in 8bjc
Zinc binding site 1 out of 1 in the Full Length Structure of the Apo-State Lpmip.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Full Length Structure of the Apo-State Lpmip. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn305

b:30.0
occ:1.00
OE2 B:GLU164 1.8 14.6 1.0
O B:HOH470 1.9 6.7 1.0
CD B:GLU164 2.5 17.0 1.0
OE1 B:GLU164 2.6 18.0 1.0
O1S B:EPE302 3.8 28.0 1.0
CG B:GLU164 4.0 12.9 1.0
O B:HOH438 4.1 17.3 1.0
O2S B:EPE302 4.2 26.9 1.0
HG3 B:GLU164 4.3 16.2 1.0
HG2 B:GLU164 4.3 16.2 1.0
HB3 B:SER106 4.4 13.8 1.0
O B:HOH420 4.5 12.7 1.0
S B:EPE302 4.5 5.1 1.0
O B:HOH506 4.7 22.7 1.0
O3S B:EPE302 4.8 20.7 1.0
HB3 B:GLU164 4.9 21.8 1.0
O B:HOH477 4.9 16.2 1.0
O B:HOH427 4.9 16.9 1.0

Reference:

C.Wiedemann, J.J.Whittaker, V.H.P.Carrillo, B.Goretzki, M.Dajka, F.Tebbe, J.M.Harder, P.R.Krajczy, B.Joseph, F.Hausch, A.Guskov, U.A.Hellmich. Legionella Pneumophila Macrophage Infectivity Potentiator Protein Appendage Domains Modulate Protein Dynamics and Inhibitor Binding. Int.J.Biol.Macromol. 26366 2023.
ISSN: ISSN 0141-8130
PubMed: 37633566
DOI: 10.1016/J.IJBIOMAC.2023.126366
Page generated: Wed Oct 30 18:21:39 2024

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