Atomistry » Manganese » PDB 1w2c-1xie » 1wlj
Atomistry »
  Manganese »
    PDB 1w2c-1xie »
      1wlj »

Manganese in PDB 1wlj: Human ISG20

Protein crystallography data

The structure of Human ISG20, PDB code: 1wlj was solved by T.Horio, M.Murai, T.Inoue, T.Hamasaki, T.Tanaka, T.Ohgi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.90
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 63.420, 63.420, 97.910, 90.00, 90.00, 120.00
R / Rfree (%) n/a / n/a

Manganese Binding Sites:

The binding sites of Manganese atom in the Human ISG20 (pdb code 1wlj). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 3 binding sites of Manganese where determined in the Human ISG20, PDB code: 1wlj:
Jump to Manganese binding site number: 1; 2; 3;

Manganese binding site 1 out of 3 in 1wlj

Go back to Manganese Binding Sites List in 1wlj
Manganese binding site 1 out of 3 in the Human ISG20


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Human ISG20 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn200

b:17.1
occ:1.00
OD2 A:ASP154 2.1 15.4 1.0
OE2 A:GLU13 2.1 16.3 1.0
OD2 A:ASP11 2.2 15.7 1.0
O2P A:U5P300 2.2 18.9 1.0
O3P A:U5P300 2.4 18.6 1.0
P A:U5P300 2.8 19.1 1.0
CD A:GLU13 3.1 16.9 1.0
CG A:ASP11 3.1 15.4 1.0
CG A:ASP154 3.2 14.8 1.0
OD1 A:ASP11 3.4 14.0 1.0
OE1 A:GLU13 3.4 18.9 1.0
CB A:ASP154 3.6 11.5 1.0
MN A:MN201 3.8 15.3 1.0
O5' A:U5P300 3.9 19.2 1.0
O A:CYS12 4.0 14.4 1.0
O1P A:U5P300 4.0 19.8 1.0
O A:HOH348 4.2 18.9 1.0
C5' A:U5P300 4.2 17.9 1.0
CB A:HIS149 4.2 20.3 1.0
OD1 A:ASP154 4.3 14.5 1.0
OE1 A:GLN143 4.3 23.5 1.0
CA A:SER151 4.4 16.6 1.0
ND1 A:HIS149 4.4 18.1 1.0
CG A:GLU13 4.5 16.4 1.0
CB A:ASP11 4.5 13.5 1.0
O A:SER150 4.6 18.2 1.0
CB A:SER151 4.7 17.4 1.0
N A:SER151 4.7 17.8 1.0
O A:HOH350 4.8 17.1 1.0
C A:CYS12 4.8 16.0 1.0
CG A:HIS149 4.8 19.0 1.0
O A:HOH321 4.8 17.5 1.0
C A:SER150 4.9 19.9 1.0

Manganese binding site 2 out of 3 in 1wlj

Go back to Manganese Binding Sites List in 1wlj
Manganese binding site 2 out of 3 in the Human ISG20


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Human ISG20 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn201

b:15.3
occ:1.00
O3P A:U5P300 2.0 18.6 1.0
OD1 A:ASP11 2.1 14.0 1.0
O A:HOH350 2.2 17.1 1.0
O A:HOH347 2.2 13.5 1.0
O A:HOH348 2.3 18.9 1.0
O A:HOH349 2.3 17.8 1.0
CG A:ASP11 3.3 15.4 1.0
P A:U5P300 3.4 19.1 1.0
OD2 A:ASP11 3.8 15.7 1.0
MN A:MN200 3.8 17.1 1.0
O1P A:U5P300 3.9 19.8 1.0
O A:HOH331 4.0 22.2 1.0
O A:HOH310 4.0 16.6 1.0
O A:HOH305 4.1 12.9 1.0
O A:CYS12 4.1 14.4 1.0
OD1 A:ASP94 4.1 27.4 1.0
C5' A:U5P300 4.2 17.9 1.0
O A:HOH321 4.2 17.5 1.0
O5' A:U5P300 4.2 19.2 1.0
O A:HIS89 4.2 16.6 1.0
OD2 A:ASP94 4.4 27.8 1.0
CB A:ASP11 4.5 13.5 1.0
O2P A:U5P300 4.5 18.9 1.0
N A:CYS12 4.6 14.3 1.0
CG A:ASP94 4.7 22.6 1.0
CA A:ASP11 4.8 15.3 1.0
O A:HOH379 4.8 39.3 1.0

Manganese binding site 3 out of 3 in 1wlj

Go back to Manganese Binding Sites List in 1wlj
Manganese binding site 3 out of 3 in the Human ISG20


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Human ISG20 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn202

b:30.5
occ:0.50
NE2 A:HIS93 2.4 28.1 1.0
OD2 A:ASP90 2.4 29.2 1.0
CD2 A:HIS93 3.1 27.3 1.0
CG A:ASP90 3.3 26.9 1.0
OD1 A:ASP90 3.4 27.3 1.0
CE1 A:HIS93 3.6 29.7 1.0
CG A:HIS93 4.3 27.3 1.0
ND1 A:HIS93 4.6 28.9 1.0
CB A:ASP90 4.6 22.3 1.0

Reference:

T.Horio, M.Murai, T.Inoue, T.Hamasaki, T.Tanaka, T.Ohgi. Crystal Structure of Human ISG20, An Interferon-Induced Antiviral Ribonuclease Febs Lett. V. 577 111 2004.
ISSN: ISSN 0014-5793
PubMed: 15527770
DOI: 10.1016/J.FEBSLET.2004.09.074
Page generated: Tue Dec 15 03:57:31 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy