Atomistry » Manganese » PDB 8kfu-8q1x » 8pzm
Atomistry »
  Manganese »
    PDB 8kfu-8q1x »
      8pzm »

Manganese in PDB 8pzm: Intracellular Leucine Aminopeptidase of Pseudomonas Aeruginosa PA14 Bound to Bestatin Inhibitor and Manganese

Protein crystallography data

The structure of Intracellular Leucine Aminopeptidase of Pseudomonas Aeruginosa PA14 Bound to Bestatin Inhibitor and Manganese, PDB code: 8pzm was solved by M.C.Simpson, C.M.Czekster, C.J.Harding, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 43.78 / 1.70
Space group P 63 2 2
Cell size a, b, c (Å), α, β, γ (°) 182.05, 182.05, 87.57, 90, 90, 120
R / Rfree (%) 17 / 18.9

Manganese Binding Sites:

The binding sites of Manganese atom in the Intracellular Leucine Aminopeptidase of Pseudomonas Aeruginosa PA14 Bound to Bestatin Inhibitor and Manganese (pdb code 8pzm). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Intracellular Leucine Aminopeptidase of Pseudomonas Aeruginosa PA14 Bound to Bestatin Inhibitor and Manganese, PDB code: 8pzm:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 8pzm

Go back to Manganese Binding Sites List in 8pzm
Manganese binding site 1 out of 2 in the Intracellular Leucine Aminopeptidase of Pseudomonas Aeruginosa PA14 Bound to Bestatin Inhibitor and Manganese


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Intracellular Leucine Aminopeptidase of Pseudomonas Aeruginosa PA14 Bound to Bestatin Inhibitor and Manganese within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn605

b:22.4
occ:1.00
OD2 A:ASP310 2.1 22.8 1.0
O2 A:BES601 2.1 22.4 1.0
OE2 A:GLU371 2.2 22.1 1.0
N2 A:BES601 2.3 23.4 1.0
NZ A:LYS287 2.3 21.7 1.0
OD2 A:ASP292 2.4 23.1 1.0
CG A:ASP310 2.9 23.6 1.0
C2 A:BES601 3.0 20.8 1.0
OD1 A:ASP310 3.0 23.2 1.0
C1 A:BES601 3.1 21.5 1.0
CE A:LYS287 3.2 21.5 1.0
CD A:GLU371 3.2 23.1 1.0
MN A:MN606 3.3 23.7 1.0
CG A:ASP292 3.3 21.2 1.0
OE1 A:GLU371 3.5 22.1 1.0
O3 A:BCT603 3.7 23.3 1.0
CB A:ASP292 3.8 22.3 1.0
O A:THR396 4.2 22.7 1.0
OD1 A:ASP292 4.3 21.3 1.0
C3 A:BES601 4.3 24.0 1.0
CB A:ASP310 4.3 21.9 1.0
C6 A:BES601 4.5 23.1 1.0
O3 A:BES601 4.5 24.0 1.0
CG A:GLU371 4.5 22.5 1.0
CD A:LYS287 4.6 22.8 1.0
CG2 A:ILE289 4.7 21.7 1.0
CB A:ILE289 4.7 23.4 1.0
N A:GLY372 4.8 22.4 1.0
CG1 A:ILE289 4.8 21.2 1.0
O A:ASP369 4.9 21.8 1.0

Manganese binding site 2 out of 2 in 8pzm

Go back to Manganese Binding Sites List in 8pzm
Manganese binding site 2 out of 2 in the Intracellular Leucine Aminopeptidase of Pseudomonas Aeruginosa PA14 Bound to Bestatin Inhibitor and Manganese


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Intracellular Leucine Aminopeptidase of Pseudomonas Aeruginosa PA14 Bound to Bestatin Inhibitor and Manganese within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn606

b:23.7
occ:1.00
OD1 A:ASP369 2.1 22.8 1.0
O A:ASP369 2.2 21.8 1.0
OD2 A:ASP292 2.2 23.1 1.0
OE1 A:GLU371 2.2 22.1 1.0
O2 A:BES601 2.2 22.4 1.0
O3 A:BES601 2.5 24.0 1.0
C3 A:BES601 3.0 24.0 1.0
CG A:ASP292 3.0 21.2 1.0
C2 A:BES601 3.0 20.8 1.0
CG A:ASP369 3.1 22.4 1.0
C A:ASP369 3.1 22.2 1.0
CD A:GLU371 3.1 23.1 1.0
OD1 A:ASP292 3.2 21.3 1.0
MN A:MN605 3.3 22.4 1.0
OE2 A:GLU371 3.4 22.1 1.0
CA A:ASP369 3.5 21.6 1.0
C1 A:BES601 3.8 21.5 1.0
NZ A:LYS299 3.8 23.2 1.0
CB A:ASP369 3.8 21.8 1.0
OD2 A:ASP369 4.0 23.0 1.0
O3 A:BCT603 4.0 23.3 1.0
CE A:LYS299 4.1 23.4 1.0
N1 A:BES601 4.1 23.3 1.0
N2 A:BES601 4.2 23.4 1.0
N A:ALA370 4.3 21.9 1.0
N A:GLU371 4.3 22.2 1.0
CB A:ASP292 4.4 22.3 1.0
CG A:GLU371 4.5 22.5 1.0
ND2 A:ASN342 4.6 22.3 1.0
CA A:ALA370 4.7 22.6 1.0
O1 A:BCT603 4.8 25.3 1.0
C4 A:BES601 4.8 23.5 1.0
CA A:GLY294 4.8 21.1 1.0
N A:ASP369 4.9 22.6 1.0
C A:BCT603 4.9 24.2 1.0
OD2 A:ASP310 4.9 22.8 1.0
CB A:GLU371 4.9 22.3 1.0

Reference:

M.C.Simpson, C.J.Harding, R.M.Czekster, L.Remmel, B.E.Bode, C.M.Czekster. Unveiling the Catalytic Mechanism of A Processive Metalloaminopeptidase. Biochemistry 2023.
ISSN: ISSN 0006-2960
PubMed: 37924287
DOI: 10.1021/ACS.BIOCHEM.3C00420
Page generated: Sun Oct 6 13:35:33 2024

Last articles

Zn in 9MJ5
Zn in 9HNW
Zn in 9G0L
Zn in 9FNE
Zn in 9DZN
Zn in 9E0I
Zn in 9D32
Zn in 9DAK
Zn in 8ZXC
Zn in 8ZUF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy