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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: Tue Aug 13 03:52:48 2024

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