Atomistry » Magnesium » PDB 7zz0-8a5p » 8a28
Atomistry »
  Magnesium »
    PDB 7zz0-8a5p »
      8a28 »

Magnesium in PDB 8a28: Structure of the Astacin Zymogen of Last-Mam From Limulus Polyphemus

Protein crystallography data

The structure of Structure of the Astacin Zymogen of Last-Mam From Limulus Polyphemus, PDB code: 8a28 was solved by T.Guevara, A.Rodriguez Banqueri, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.73 / 2.40
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 115.83, 47.57, 236.4, 90, 102.91, 90
R / Rfree (%) 25.3 / 28.9

Other elements in 8a28:

The structure of Structure of the Astacin Zymogen of Last-Mam From Limulus Polyphemus also contains other interesting chemical elements:

Zinc (Zn) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of the Astacin Zymogen of Last-Mam From Limulus Polyphemus (pdb code 8a28). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Structure of the Astacin Zymogen of Last-Mam From Limulus Polyphemus, PDB code: 8a28:

Magnesium binding site 1 out of 1 in 8a28

Go back to Magnesium Binding Sites List in 8a28
Magnesium binding site 1 out of 1 in the Structure of the Astacin Zymogen of Last-Mam From Limulus Polyphemus


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of the Astacin Zymogen of Last-Mam From Limulus Polyphemus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg502

b:47.4
occ:1.00
O A:HIS31 2.0 65.2 1.0
O A:LEU34 2.8 47.9 1.0
C A:HIS31 3.2 63.9 1.0
O A:SER32 3.4 62.9 1.0
C A:SER32 3.6 62.2 1.0
CA A:SER32 3.6 63.2 1.0
N A:GLY37 3.7 43.9 1.0
ND2 A:ASN174 3.7 54.8 1.0
CA A:GLY37 3.7 43.4 1.0
N A:SER32 3.8 63.4 1.0
C A:LEU34 4.0 49.8 1.0
CE A:MET171 4.0 55.2 1.0
SD A:MET171 4.0 70.1 1.0
CE1 A:PHE203 4.0 52.0 1.0
N A:LEU34 4.0 52.0 1.0
CA A:HIS31 4.4 61.1 1.0
N A:HIS31 4.5 57.0 1.0
CA A:LEU34 4.5 49.4 1.0
N A:ASN33 4.5 60.7 1.0
CG A:ASN174 4.6 54.6 1.0
OD1 A:ASN174 4.6 57.0 1.0
CZ A:PHE203 4.6 53.0 1.0
C A:GLY37 4.7 44.1 1.0
C A:GLU36 4.9 45.4 1.0
C A:TYR30 4.9 54.3 1.0
O A:GLY37 4.9 46.3 1.0
CD1 A:PHE203 4.9 51.4 1.0
N A:GLU36 5.0 49.3 1.0

Reference:

T.Guevara, A.Rodriguez-Banqueri, M.Ksiazek, J.Potempa, F.X.Gomis-Ruth. Structure-Based Mechanism of Cysteine-Switch Latency and of Catalysis By Pappalysin-Family Metallopeptidases Iucrj V. 7 18 2020.
ISSN: ESSN 2052-2525
DOI: 10.1107/S2059798322009688
Page generated: Thu Oct 3 17:10:26 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy