Atomistry » Magnesium » PDB 1gpm-1h7l » 1h3i
Atomistry »
  Magnesium »
    PDB 1gpm-1h7l »
      1h3i »

Magnesium in PDB 1h3i: Crystal Structure of the Histone Methyltransferase SET7/9

Enzymatic activity of Crystal Structure of the Histone Methyltransferase SET7/9

All present enzymatic activity of Crystal Structure of the Histone Methyltransferase SET7/9:
2.1.1.43;

Protein crystallography data

The structure of Crystal Structure of the Histone Methyltransferase SET7/9, PDB code: 1h3i was solved by J.R.Wilson, C.Jing, P.A.Walker, S.R.Martin, S.A.Howell, G.M.Blackburn, S.J.Gamblin, B.Xiao, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.1
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 66.090, 82.830, 116.150, 90.00, 90.00, 90.00
R / Rfree (%) 21 / 25.5

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Histone Methyltransferase SET7/9 (pdb code 1h3i). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Crystal Structure of the Histone Methyltransferase SET7/9, PDB code: 1h3i:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in 1h3i

Go back to Magnesium Binding Sites List in 1h3i
Magnesium binding site 1 out of 3 in the Crystal Structure of the Histone Methyltransferase SET7/9


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of the Histone Methyltransferase SET7/9 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1345

b:21.1
occ:1.00
O A:HOH2133 2.0 14.3 1.0
O A:HOH2147 2.0 20.3 1.0
O A:HOH2149 2.1 15.6 1.0
O A:HOH2134 2.2 22.5 1.0
O A:HOH2150 2.6 21.3 1.0
OD1 A:ASN296 4.0 17.8 1.0
O A:HOH2135 4.1 23.2 1.0
NE2 A:HIS339 4.1 19.9 1.0
ND1 A:HIS297 4.2 12.8 1.0
O A:HOH2120 4.2 36.2 1.0
OD1 A:ASN265 4.3 20.9 1.0
O A:GLY264 4.3 14.8 1.0
O A:HIS293 4.3 12.7 1.0
CE1 A:HIS339 4.5 19.4 1.0
CE1 A:HIS297 4.5 17.1 1.0
O A:ALA295 4.6 17.2 1.0
CA A:ASN296 4.8 14.2 1.0
CD2 A:HIS339 4.8 15.7 1.0
O A:HOH2116 5.0 20.1 1.0

Magnesium binding site 2 out of 3 in 1h3i

Go back to Magnesium Binding Sites List in 1h3i
Magnesium binding site 2 out of 3 in the Crystal Structure of the Histone Methyltransferase SET7/9


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of the Histone Methyltransferase SET7/9 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1346

b:2.0
occ:1.00
OE1 B:GLU279 2.0 20.1 1.0
NE2 B:HIS283 2.0 15.2 1.0
CD B:GLU279 2.7 9.9 1.0
CE1 B:HIS283 2.9 17.9 1.0
OE2 B:GLU279 2.9 7.2 1.0
CD2 B:HIS283 3.1 8.5 1.0
CG B:GLU279 3.9 14.1 1.0
OD1 B:ASN282 4.0 12.7 1.0
ND1 B:HIS283 4.0 18.1 1.0
CG B:HIS283 4.2 10.8 1.0
O B:GLU279 4.3 27.9 1.0
ND2 B:ASN282 4.4 2.0 1.0
CG B:ASN282 4.6 10.0 1.0

Magnesium binding site 3 out of 3 in 1h3i

Go back to Magnesium Binding Sites List in 1h3i
Magnesium binding site 3 out of 3 in the Crystal Structure of the Histone Methyltransferase SET7/9


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of the Histone Methyltransferase SET7/9 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg1346

b:21.9
occ:1.00
O B:HOH2125 1.8 22.5 1.0
O B:HOH2123 1.9 17.1 1.0
O B:HOH2141 1.9 18.2 1.0
O B:HOH2140 2.0 18.4 1.0
O B:HOH2143 2.1 24.8 1.0
O B:HOH2043 4.0 35.6 1.0
OD1 B:ASN265 4.0 13.8 1.0
O B:GLY264 4.1 7.6 1.0
O B:HOH2100 4.1 15.4 1.0
O B:HIS293 4.2 7.5 1.0
O B:HOH2111 4.2 25.5 1.0
O B:HOH2142 4.2 24.6 1.0
OD1 B:ASN296 4.3 14.6 1.0
NE2 B:HIS339 4.4 17.0 1.0
ND1 B:HIS297 4.4 11.2 1.0
O B:ALA295 4.4 5.5 1.0
CE1 B:HIS297 4.6 11.5 1.0
O B:HOH2042 4.6 33.3 1.0
O B:HOH2102 4.8 31.4 1.0
CE1 B:HIS339 4.9 8.7 1.0
CA B:ASN296 4.9 8.6 1.0

Reference:

J.R.Wilson, C.Jing, P.A.Walker, S.R.Martin, S.A.Howell, G.M.Blackburn, S.J.Gamblin, B.Xiao. Crystal Structure and Functional Analysis of the Histone Methyltransferase SET7/9 Cell(Cambridge,Mass.) V. 111 105 2002.
ISSN: ISSN 0092-8674
PubMed: 12372304
DOI: 10.1016/S0092-8674(02)00964-9
Page generated: Mon Dec 14 05:58:37 2020

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy