Atomistry » Zinc » PDB 3blo-3c37 » 3bo5
Atomistry »
  Zinc »
    PDB 3blo-3c37 »
      3bo5 »

Zinc in PDB 3bo5: Crystal Structure of Methyltransferase Domain of Human Histone-Lysine N-Methyltransferase Setmar

Enzymatic activity of Crystal Structure of Methyltransferase Domain of Human Histone-Lysine N-Methyltransferase Setmar

All present enzymatic activity of Crystal Structure of Methyltransferase Domain of Human Histone-Lysine N-Methyltransferase Setmar:
2.1.1.43;

Protein crystallography data

The structure of Crystal Structure of Methyltransferase Domain of Human Histone-Lysine N-Methyltransferase Setmar, PDB code: 3bo5 was solved by V.V.Lunin, H.Wu, H.Ren, E.Dobrovetsky, J.Weigelt, C.H.Arrowsmith, A.M.Edwards, A.Bochkarev, J.Min, A.N.Plotnikov, Structural Genomicsconsortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.91 / 1.59
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 41.396, 67.827, 44.637, 90.00, 105.93, 90.00
R / Rfree (%) 15.5 / 19.9

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Methyltransferase Domain of Human Histone-Lysine N-Methyltransferase Setmar (pdb code 3bo5). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Crystal Structure of Methyltransferase Domain of Human Histone-Lysine N-Methyltransferase Setmar, PDB code: 3bo5:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 3bo5

Go back to Zinc Binding Sites List in 3bo5
Zinc binding site 1 out of 4 in the Crystal Structure of Methyltransferase Domain of Human Histone-Lysine N-Methyltransferase Setmar


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Methyltransferase Domain of Human Histone-Lysine N-Methyltransferase Setmar within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:13.7
occ:1.00
 SG A:CYS75 2.3 13.7 1.0
SG A:CYS104 2.4 12.7 1.0
SG A:CYS108 2.4 13.3 1.0
SG A:CYS61 2.4 14.0 1.0
CB A:CYS104 3.1 14.6 1.0
CB A:CYS61 3.2 15.4 1.0
CB A:CYS75 3.3 15.2 1.0
CB A:CYS108 3.3 14.5 1.0
CA A:CYS104 3.4 12.7 1.0
N A:CYS61 3.5 16.6 1.0
ZN A:ZN303 3.7 14.2 1.0
ZN A:ZN302 3.9 14.7 1.0
CA A:CYS61 4.0 16.7 1.0
SG A:CYS73 4.1 15.4 1.0
N A:CYS104 4.3 10.7 1.0
SG A:CYS110 4.5 15.8 1.0
C A:CYS104 4.6 13.3 1.0
N A:ASN105 4.6 13.6 1.0
CA A:CYS108 4.6 14.9 1.0
C A:GLY60 4.6 18.7 1.0
CA A:CYS75 4.6 14.2 1.0
SG A:CYS68 4.6 14.9 1.0
N A:CYS75 4.7 15.4 1.0
CA A:GLY60 4.8 16.6 1.0
C A:CYS61 4.9 16.5 1.0
O A:GLU103 5.0 13.9 1.0

Zinc binding site 2 out of 4 in 3bo5

Go back to Zinc Binding Sites List in 3bo5
Zinc binding site 2 out of 4 in the Crystal Structure of Methyltransferase Domain of Human Histone-Lysine N-Methyltransferase Setmar


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Methyltransferase Domain of Human Histone-Lysine N-Methyltransferase Setmar within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn302

b:14.7
occ:1.00
 SG A:CYS110 2.3 15.8 1.0
SG A:CYS114 2.3 14.5 1.0
SG A:CYS104 2.4 12.7 1.0
SG A:CYS68 2.4 14.9 1.0
CB A:CYS110 3.1 19.6 1.0
CB A:CYS104 3.1 14.6 1.0
CB A:CYS114 3.3 15.7 1.0
CB A:CYS68 3.3 13.9 1.0
ZN A:ZN301 3.9 13.7 1.0
ZN A:ZN303 4.0 14.2 1.0
O A:HOH443 4.1 18.0 1.0
SG A:CYS61 4.3 14.0 1.0
CA A:CYS110 4.5 19.1 1.0
CA A:CYS104 4.6 12.7 1.0
CA A:CYS68 4.7 15.0 1.0
CA A:CYS114 4.7 16.1 1.0
CB A:ASN116 4.7 12.9 1.0
NE A:ARG117 4.7 15.6 1.0
CB A:CYS108 4.8 14.5 1.0
O A:HOH499 4.9 26.7 1.0
N A:CYS68 4.9 16.0 1.0
SG A:CYS73 5.0 15.4 1.0

Zinc binding site 3 out of 4 in 3bo5

Go back to Zinc Binding Sites List in 3bo5
Zinc binding site 3 out of 4 in the Crystal Structure of Methyltransferase Domain of Human Histone-Lysine N-Methyltransferase Setmar


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of Methyltransferase Domain of Human Histone-Lysine N-Methyltransferase Setmar within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn303

b:14.2
occ:1.00
 SG A:CYS73 2.3 15.4 1.0
SG A:CYS63 2.3 15.0 1.0
SG A:CYS61 2.4 14.0 1.0
SG A:CYS68 2.4 14.9 1.0
CB A:CYS61 3.1 15.4 1.0
CB A:CYS73 3.2 17.3 1.0
CB A:CYS68 3.2 13.9 1.0
CB A:CYS63 3.2 12.6 1.0
ZN A:ZN301 3.7 13.7 1.0
CA A:CYS73 3.8 16.9 1.0
CA A:CYS68 3.8 15.0 1.0
ZN A:ZN302 4.0 14.7 1.0
SG A:CYS104 4.2 12.7 1.0
N A:CYS63 4.3 17.4 1.0
CA A:CYS63 4.4 16.4 1.0
CA A:CYS61 4.5 16.7 1.0
C A:CYS73 4.5 16.4 1.0
O A:HOH562 4.6 17.6 1.0
O A:HOH465 4.7 20.4 1.0
N A:SER74 4.7 17.1 1.0
N A:CYS68 4.7 16.0 1.0
C A:CYS61 4.9 16.5 1.0
N A:ILE62 4.9 16.3 1.0
CB A:CYS75 4.9 15.2 1.0
SG A:CYS75 4.9 13.7 1.0
C A:CYS68 5.0 17.1 1.0
N A:CYS73 5.0 17.9 1.0

Zinc binding site 4 out of 4 in 3bo5

Go back to Zinc Binding Sites List in 3bo5
Zinc binding site 4 out of 4 in the Crystal Structure of Methyltransferase Domain of Human Histone-Lysine N-Methyltransferase Setmar


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of Methyltransferase Domain of Human Histone-Lysine N-Methyltransferase Setmar within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn304

b:14.2
occ:1.00
 SG A:CYS275 2.3 14.1 1.0
SG A:CYS280 2.3 16.4 1.0
SG A:CYS273 2.4 13.8 1.0
SG A:CYS212 2.4 15.2 1.0
CB A:CYS275 3.3 16.7 1.0
CB A:CYS280 3.3 19.9 1.0
CB A:CYS212 3.3 15.1 1.0
CB A:CYS273 3.4 13.8 1.0
CA A:CYS280 3.7 19.9 1.0
N A:CYS212 3.8 13.0 1.0
N A:CYS275 3.9 14.9 1.0
CA A:CYS275 4.2 13.5 1.0
N A:THR281 4.2 19.8 1.0
CA A:CYS212 4.3 14.0 1.0
O A:HOH416 4.4 18.6 1.0
NE2 A:HIS210 4.5 12.1 1.0
CD2 A:HIS210 4.5 14.3 1.0
C A:CYS280 4.5 19.7 1.0
CA A:CYS273 4.6 13.3 1.0
C A:CYS273 4.6 14.0 1.0
O A:CYS273 4.7 15.9 1.0
N A:ALA282 4.7 17.8 1.0
N A:GLY276 4.8 14.8 1.0
C A:CYS275 4.8 15.2 1.0
C A:SER211 4.9 12.3 1.0
N A:CYS280 4.9 19.6 1.0
N A:TYR274 4.9 13.7 1.0
OG1 A:THR281 5.0 20.8 1.0

Reference:

H.Wu, V.V.Lunin, H.Ren, E.Dobrovetsky, J.Weigelt, C.H.Arrowsmith, A.M.Edwards, A.Bochkarev, J.Min, A.N.Plotnikov. The Crystal Structure of Methyltransferase Domain of Human Histone-Lysine N-Methyltransferase Setmar in Complex with Adohcy. To Be Published.
Page generated: Thu Oct 24 11:35:34 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy