Atomistry » Zinc » PDB 3ojg-3ox1 » 3ope
Atomistry »
  Zinc »
    PDB 3ojg-3ox1 »
      3ope »

Zinc in PDB 3ope: Structural Basis of Auto-Inhibitory Mechanism of Histone Methyltransferase

Enzymatic activity of Structural Basis of Auto-Inhibitory Mechanism of Histone Methyltransferase

All present enzymatic activity of Structural Basis of Auto-Inhibitory Mechanism of Histone Methyltransferase:
2.1.1.43;

Protein crystallography data

The structure of Structural Basis of Auto-Inhibitory Mechanism of Histone Methyltransferase, PDB code: 3ope was solved by S.An, J.Song, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.90
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 59.530, 59.530, 233.804, 90.00, 90.00, 120.00
R / Rfree (%) 23.5 / 29.9

Zinc Binding Sites:

The binding sites of Zinc atom in the Structural Basis of Auto-Inhibitory Mechanism of Histone Methyltransferase (pdb code 3ope). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 6 binding sites of Zinc where determined in the Structural Basis of Auto-Inhibitory Mechanism of Histone Methyltransferase, PDB code: 3ope:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6;

Zinc binding site 1 out of 6 in 3ope

Go back to Zinc Binding Sites List in 3ope
Zinc binding site 1 out of 6 in the Structural Basis of Auto-Inhibitory Mechanism of Histone Methyltransferase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structural Basis of Auto-Inhibitory Mechanism of Histone Methyltransferase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1

b:74.6
occ:0.87
CB A:CYS2270 2.3 52.5 1.0
SG A:CYS2220 2.4 60.0 1.0
SG A:CYS2268 2.5 58.2 1.0
SG A:CYS2275 2.6 61.6 1.0
SG A:CYS2270 2.7 53.8 1.0
CB A:CYS2275 3.4 63.9 1.0
CB A:CYS2220 3.6 58.1 1.0
CB A:CYS2268 3.6 59.0 1.0
CA A:CYS2270 3.7 53.2 1.0
N A:CYS2220 4.0 57.0 1.0
CA A:CYS2275 4.0 64.5 1.0
N A:CYS2270 4.1 53.0 1.0
N A:ARG2276 4.3 64.5 1.0
CA A:CYS2220 4.4 58.4 1.0
O A:CYS2268 4.5 61.6 1.0
C A:CYS2275 4.5 64.6 1.0
C A:CYS2270 4.6 54.9 1.0
CE1 A:HIS2218 4.6 59.8 1.0
C A:CYS2268 4.7 60.3 1.0
N A:GLY2277 4.7 63.7 1.0
CA A:CYS2268 4.8 60.8 1.0
ND1 A:HIS2218 4.8 57.8 1.0
N A:GLY2271 4.8 58.2 1.0
C A:SER2219 4.9 56.1 1.0
CB A:PHE2272 5.0 67.0 1.0

Zinc binding site 2 out of 6 in 3ope

Go back to Zinc Binding Sites List in 3ope
Zinc binding site 2 out of 6 in the Structural Basis of Auto-Inhibitory Mechanism of Histone Methyltransferase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structural Basis of Auto-Inhibitory Mechanism of Histone Methyltransferase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn2

b:86.9
occ:0.71
SG A:CYS2122 2.3 86.4 1.0
SG A:CYS2117 2.5 88.3 1.0
SG A:CYS2128 2.7 72.4 1.0
CB A:CYS2117 3.0 81.4 1.0
SG A:CYS2091 3.1 98.9 1.0
CB A:CYS2122 3.4 83.8 1.0
SG A:CYS2104 3.7 0.2 1.0
CB A:CYS2128 4.0 76.0 1.0
ZN A:ZN4 4.0 71.1 0.6
CB A:ASN2130 4.1 63.5 1.0
CB A:CYS2091 4.2 0.8 1.0
CA A:CYS2117 4.4 76.2 1.0
CB A:CYS2104 4.5 0.6 1.0
CA A:CYS2122 4.6 82.9 1.0
N A:ASN2130 4.7 67.1 1.0
NE2 A:GLN2131 4.7 68.6 1.0
N A:CYS2117 4.8 71.9 1.0
CA A:ASN2130 4.8 65.3 1.0
CG A:GLN2131 4.9 65.2 1.0
O A:ASN2130 4.9 65.7 1.0
OD1 A:ASN2130 5.0 63.9 1.0

Zinc binding site 3 out of 6 in 3ope

Go back to Zinc Binding Sites List in 3ope
Zinc binding site 3 out of 6 in the Structural Basis of Auto-Inhibitory Mechanism of Histone Methyltransferase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Structural Basis of Auto-Inhibitory Mechanism of Histone Methyltransferase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn4

b:71.1
occ:0.60
SG A:CYS2104 2.3 0.2 1.0
SG A:CYS2093 2.5 0.0 1.0
CB A:CYS2108 2.5 0.8 1.0
CB A:CYS2091 2.7 0.8 1.0
SG A:CYS2091 2.8 98.9 1.0
SG A:CYS2108 2.8 0.1 1.0
CB A:CYS2093 3.0 0.9 1.0
O A:CYS2091 3.0 0.3 1.0
N A:CYS2093 3.4 0.3 1.0
C A:CYS2091 3.4 0.3 1.0
CA A:CYS2108 3.4 0.5 1.0
CA A:CYS2091 3.6 0.4 1.0
CA A:CYS2093 3.7 0.9 1.0
ZN A:ZN2 4.0 86.9 0.7
O A:CYS2093 4.1 0.8 1.0
CB A:CYS2104 4.1 0.6 1.0
C A:CYS2108 4.2 0.2 1.0
N A:ASN2092 4.2 0.1 1.0
SG A:CYS2117 4.3 88.3 1.0
C A:CYS2093 4.4 0.0 1.0
C A:ASN2092 4.4 0.3 1.0
N A:CYS2108 4.6 0.1 1.0
O A:CYS2108 4.7 0.8 1.0
N A:CYS2091 4.8 0.7 1.0
N A:LEU2109 4.8 0.4 1.0
CA A:ASN2092 4.9 0.6 1.0
SG A:CYS2122 4.9 86.4 1.0
CA A:CYS2104 5.0 0.6 1.0

Zinc binding site 4 out of 6 in 3ope

Go back to Zinc Binding Sites List in 3ope
Zinc binding site 4 out of 6 in the Structural Basis of Auto-Inhibitory Mechanism of Histone Methyltransferase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Structural Basis of Auto-Inhibitory Mechanism of Histone Methyltransferase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn3

b:72.8
occ:0.64
CB B:CYS2268 2.2 97.3 1.0
SG B:CYS2220 2.2 93.5 1.0
CB B:CYS2220 2.4 85.5 1.0
SG B:CYS2268 2.9 97.3 1.0
CA B:CYS2220 3.3 80.8 1.0
CB B:CYS2275 3.4 0.9 1.0
SG B:CYS2275 3.5 100.0 1.0
CA B:CYS2268 3.6 97.2 1.0
N B:GLY2277 3.6 95.9 1.0
CE1 B:HIS2218 3.8 63.3 1.0
C B:CYS2275 3.9 99.7 1.0
N B:CYS2220 3.9 78.2 1.0
CA B:CYS2275 3.9 0.4 1.0
SG B:CYS2270 3.9 96.6 1.0
N B:ARG2276 4.1 98.2 1.0
CA B:GLY2277 4.1 95.4 1.0
N B:CYS2268 4.2 98.9 1.0
O B:CYS2275 4.2 0.8 1.0
O B:GLY2277 4.3 94.6 1.0
ND1 B:HIS2218 4.4 62.6 1.0
C B:GLY2277 4.6 94.9 1.0
C B:CYS2220 4.6 79.3 1.0
C B:ARG2276 4.6 96.3 1.0
C B:CYS2268 4.7 96.5 1.0
CA B:ARG2276 4.8 96.9 1.0
NE2 B:HIS2218 4.9 64.0 1.0
C B:SER2219 4.9 74.9 1.0
CB B:ARG2276 4.9 96.6 1.0
O B:CYS2268 5.0 96.8 1.0

Zinc binding site 5 out of 6 in 3ope

Go back to Zinc Binding Sites List in 3ope
Zinc binding site 5 out of 6 in the Structural Basis of Auto-Inhibitory Mechanism of Histone Methyltransferase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Structural Basis of Auto-Inhibitory Mechanism of Histone Methyltransferase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn5

b:81.1
occ:0.51
SG B:CYS2122 2.1 99.0 1.0
SG B:CYS2128 2.4 96.4 1.0
SG B:CYS2117 2.7 81.3 1.0
ZN B:ZN6 3.0 83.7 0.5
CB B:CYS2122 3.6 98.9 1.0
CB B:CYS2117 3.7 78.6 1.0
CB B:CYS2128 3.9 96.2 1.0
SG B:CYS2104 4.1 0.7 1.0
CB B:CYS2124 4.1 0.9 1.0
CA B:CYS2122 4.4 99.8 1.0
CA B:CYS2128 4.4 96.5 1.0
SG B:CYS2124 4.7 97.8 1.0
SG B:CYS2108 4.9 96.3 1.0
NE2 B:GLN2131 5.0 68.5 1.0

Zinc binding site 6 out of 6 in 3ope

Go back to Zinc Binding Sites List in 3ope
Zinc binding site 6 out of 6 in the Structural Basis of Auto-Inhibitory Mechanism of Histone Methyltransferase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Structural Basis of Auto-Inhibitory Mechanism of Histone Methyltransferase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn6

b:83.7
occ:0.50
SG B:CYS2108 2.6 96.3 1.0
SG B:CYS2104 2.8 0.7 1.0
CB B:CYS2104 2.9 0.1 1.0
ZN B:ZN5 3.0 81.1 0.5
CB B:CYS2108 3.4 99.0 1.0
SG B:CYS2117 3.8 81.3 1.0
CA B:CYS2104 4.4 0.2 1.0
CA B:CYS2108 4.5 99.7 1.0
O B:CYS2104 4.7 0.7 1.0
O B:ASP2107 4.9 0.1 1.0

Reference:

S.An, K.J.Yeo, Y.H.Jeon, J.Song. Crystal Structure of the Human Histone Methyltransferase ASH1L Catalytic Domain and Its Implications For the Regulatory Mechanism J.Biol.Chem. V. 286 8369 2011.
ISSN: ISSN 0021-9258
PubMed: 21239497
DOI: 10.1074/JBC.M110.203380
Page generated: Wed Dec 16 04:41:03 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