Atomistry » Magnesium » PDB 5osf-5p9r » 5ouo
Atomistry »
  Magnesium »
    PDB 5osf-5p9r »
      5ouo »

Magnesium in PDB 5ouo: Structure of TGPLP1 Apcbeta Domain

Protein crystallography data

The structure of Structure of TGPLP1 Apcbeta Domain, PDB code: 5ouo was solved by T.Ni, R.J.C.Gilbert, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.37 / 1.11
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 100.760, 50.210, 52.280, 90.00, 90.96, 90.00
R / Rfree (%) 14.9 / 16.7

Other elements in 5ouo:

The structure of Structure of TGPLP1 Apcbeta Domain also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of TGPLP1 Apcbeta Domain (pdb code 5ouo). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of TGPLP1 Apcbeta Domain, PDB code: 5ouo:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 5ouo

Go back to Magnesium Binding Sites List in 5ouo
Magnesium binding site 1 out of 2 in the Structure of TGPLP1 Apcbeta Domain


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of TGPLP1 Apcbeta Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1101

b:15.8
occ:1.00
H A:ASN983 2.2 12.3 1.0
H A:THR948 2.4 11.1 1.0
HA A:VAL982 2.8 14.2 1.0
O A:HOH1396 2.8 20.9 1.0
HD22 A:ASN983 3.0 13.4 1.0
HA A:THR947 3.0 11.6 1.0
HG23 A:VAL982 3.0 18.6 1.0
N A:ASN983 3.0 10.3 1.0
O A:HOH1235 3.0 27.8 1.0
HG23 A:THR947 3.2 14.6 1.0
HB2 A:ASN983 3.2 12.2 1.0
N A:THR948 3.2 9.2 1.0
HB A:THR948 3.4 11.2 1.0
OG1 A:THR948 3.4 10.9 1.0
CA A:VAL982 3.6 11.8 1.0
CG2 A:VAL982 3.8 15.5 1.0
ND2 A:ASN983 3.8 11.1 1.0
HG22 A:VAL982 3.8 18.6 1.0
CB A:THR948 3.8 9.3 1.0
C A:VAL982 3.8 12.6 1.0
CA A:THR947 3.8 9.7 1.0
CB A:ASN983 3.9 10.1 1.0
CG2 A:THR947 4.0 12.1 1.0
CA A:ASN983 4.0 10.0 1.0
C A:THR947 4.0 9.6 1.0
HG22 A:THR947 4.1 14.6 1.0
HG1 A:THR948 4.1 13.0 1.0
CA A:THR948 4.1 8.9 1.0
O A:ASN983 4.2 11.5 1.0
CB A:VAL982 4.2 14.3 1.0
HG1 A:THR947 4.2 17.2 1.0
CG A:ASN983 4.4 9.7 1.0
HD21 A:ASN983 4.4 13.4 1.0
O A:CYS946 4.4 14.2 1.0
CB A:THR947 4.4 9.9 1.0
HB A:VAL982 4.5 17.2 1.0
O A:LEU981 4.5 14.6 1.0
HG21 A:VAL982 4.6 18.6 1.0
C A:ASN983 4.6 9.8 1.0
O A:HOH1254 4.7 24.8 1.0
N A:VAL982 4.7 11.9 1.0
HB3 A:ASN983 4.7 12.2 1.0
HG21 A:THR947 4.7 14.6 1.0
HA A:ASN983 4.8 12.0 1.0
OG1 A:THR947 4.8 14.3 1.0
O A:THR948 4.8 10.6 1.0
HA A:THR948 4.8 10.7 1.0
N A:THR947 5.0 9.8 1.0
C A:THR948 5.0 9.8 1.0

Magnesium binding site 2 out of 2 in 5ouo

Go back to Magnesium Binding Sites List in 5ouo
Magnesium binding site 2 out of 2 in the Structure of TGPLP1 Apcbeta Domain


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of TGPLP1 Apcbeta Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1102

b:30.8
occ:0.65
O A:HOH1229 1.9 45.2 1.0
OE1 A:GLU986 2.2 22.1 1.0
O A:HOH1473 2.2 43.3 1.0
O A:HOH1244 2.2 33.9 1.0
O A:HOH1471 2.3 47.7 1.0
CD A:GLU986 3.1 33.7 1.0
O A:HOH1418 3.3 30.7 1.0
OE2 A:GLU986 3.4 20.7 1.0
H A:LEU987 4.0 13.9 1.0
O A:HOH1433 4.0 35.5 1.0
HA A:GLU986 4.0 13.7 1.0
O A:HOH1587 4.1 48.1 1.0
O A:LEU987 4.3 12.5 1.0
CG A:GLU986 4.5 17.3 1.0
N A:LEU987 4.6 11.6 1.0
HB2 A:GLU986 4.7 15.8 1.0
HG3 A:GLU986 4.8 20.7 1.0
CA A:GLU986 4.8 11.4 1.0
CB A:GLU986 4.9 13.1 1.0

Reference:

T.Ni, S.I.Williams, S.Rezelj, G.Anderluh, K.Harlos, P.J.Stansfeld, R.J.C.Gilbert. Structures of Monomeric and Oligomeric Forms of Thetoxoplasma Gondiiperforin-Like Protein 1. Sci Adv V. 4 Q0762 2018.
ISSN: ESSN 2375-2548
PubMed: 29750191
DOI: 10.1126/SCIADV.AAQ0762
Page generated: Mon Sep 30 01:23:41 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