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Zinc in PDB 6ago: Crystal Structure of MRG15-ASH1L Histone Methyltransferase Complex

Enzymatic activity of Crystal Structure of MRG15-ASH1L Histone Methyltransferase Complex

All present enzymatic activity of Crystal Structure of MRG15-ASH1L Histone Methyltransferase Complex:
2.1.1.43;

Protein crystallography data

The structure of Crystal Structure of MRG15-ASH1L Histone Methyltransferase Complex, PDB code: 6ago was solved by Y.Lee, J.Song, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 33.92 / 3.10
Space group P 31 1 2
Cell size a, b, c (Å), α, β, γ (°) 115.757, 115.757, 209.282, 90.00, 90.00, 120.00
R / Rfree (%) 22 / 27.2

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of MRG15-ASH1L Histone Methyltransferase Complex (pdb code 6ago). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 6 binding sites of Zinc where determined in the Crystal Structure of MRG15-ASH1L Histone Methyltransferase Complex, PDB code: 6ago:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6;

Zinc binding site 1 out of 6 in 6ago

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Zinc binding site 1 out of 6 in the Crystal Structure of MRG15-ASH1L Histone Methyltransferase Complex


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 MRG15-ASH1L Histone Methyltransferase Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn2302

b:0.2
occ:1.00
 SG A:CYS2270 2.4 0.9 1.0
SG A:CYS2220 2.4 0.1 1.0
SG A:CYS2275 2.6 0.8 1.0
CB A:CYS2270 2.9 0.9 1.0
SG A:CYS2268 3.3 0.1 1.0
CB A:CYS2220 3.6 0.1 1.0
CB A:CYS2275 3.6 0.6 1.0
N A:CYS2220 3.9 0.5 1.0
N A:CYS2270 3.9 0.0 1.0
CA A:CYS2275 3.9 0.1 1.0
CA A:CYS2270 4.0 0.3 1.0
N A:ARG2276 4.1 0.1 1.0
CA A:CYS2220 4.3 0.3 1.0
C A:CYS2275 4.5 0.3 1.0
N A:GLY2271 4.5 0.9 1.0
C A:CYS2270 4.7 0.2 1.0
CB A:CYS2268 4.9 0.5 1.0
N A:PHE2272 4.9 0.9 1.0
NE2 A:HIS2218 4.9 0.8 1.0
C A:SER2219 4.9 0.6 1.0
CB A:PHE2272 4.9 0.1 1.0

Zinc binding site 2 out of 6 in 6ago

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Zinc binding site 2 out of 6 in the Crystal Structure of MRG15-ASH1L Histone Methyltransferase Complex


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 MRG15-ASH1L Histone Methyltransferase Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn2303

b:0.3
occ:1.00
 SG A:CYS2091 2.4 95.7 1.0
SG A:CYS2108 2.4 1.0 1.0
SG A:CYS2104 2.4 0.8 1.0
SG A:CYS2093 2.5 0.7 1.0
CB A:CYS2108 2.7 97.4 1.0
CB A:CYS2091 2.9 0.8 1.0
CB A:CYS2104 2.9 0.3 1.0
CB A:CYS2093 3.5 0.1 1.0
CA A:CYS2108 3.6 0.3 1.0
ZN A:ZN2304 3.6 0.2 1.0
CA A:CYS2104 3.7 0.8 1.0
SG A:CYS2117 4.0 96.0 1.0
CA A:CYS2091 4.3 0.6 1.0
N A:LEU2109 4.4 0.6 1.0
C A:CYS2108 4.4 0.5 1.0
O A:CYS2091 4.6 0.3 1.0
N A:CYS2104 4.6 0.9 1.0
N A:CYS2108 4.7 1.0 1.0
C A:CYS2091 4.7 0.0 1.0
CA A:CYS2093 4.7 0.7 1.0
N A:CYS2093 4.7 0.3 1.0
C A:CYS2104 4.8 0.9 1.0

Zinc binding site 3 out of 6 in 6ago

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Zinc binding site 3 out of 6 in the Crystal Structure of MRG15-ASH1L Histone Methyltransferase Complex


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 MRG15-ASH1L Histone Methyltransferase Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn2304

b:0.2
occ:1.00
 SG A:CYS2122 2.3 98.1 1.0
SG A:CYS2117 2.4 96.0 1.0
SG A:CYS2104 2.5 0.8 1.0
SG A:CYS2128 2.5 1.0 1.0
CB A:CYS2117 3.1 99.0 1.0
CB A:CYS2122 3.5 89.2 1.0
CB A:CYS2104 3.6 0.3 1.0
CB A:CYS2128 3.6 93.8 1.0
SG A:CYS2091 3.6 95.7 1.0
ZN A:ZN2303 3.6 0.3 1.0
CB A:ASN2130 4.4 1.0 1.0
CA A:CYS2128 4.5 0.5 1.0
CA A:CYS2117 4.6 84.2 1.0
CA A:CYS2122 4.6 92.2 1.0
CB A:CYS2124 4.7 0.8 1.0
NE2 A:GLN2131 4.9 0.7 1.0
SG A:CYS2108 4.9 1.0 1.0
N A:ASN2130 5.0 97.6 1.0
CA A:CYS2104 5.0 0.8 1.0

Zinc binding site 4 out of 6 in 6ago

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Zinc binding site 4 out of 6 in the Crystal Structure of MRG15-ASH1L Histone Methyltransferase Complex


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 MRG15-ASH1L Histone Methyltransferase Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn2301

b:0.9
occ:1.00
 SG B:CYS2270 2.5 0.5 1.0
CB B:CYS2270 2.7 0.4 1.0
N B:CYS2270 3.2 0.1 1.0
CA B:CYS2275 3.4 0.6 1.0
O B:CYS2268 3.4 0.5 1.0
O B:CYS2275 3.5 0.3 1.0
CA B:CYS2270 3.5 0.1 1.0
SG B:CYS2220 3.5 0.5 1.0
SG B:CYS2275 3.6 0.9 1.0
CB B:CYS2275 3.8 0.3 1.0
C B:CYS2275 3.9 0.6 1.0
C B:CYS2268 4.0 0.4 1.0
C B:LYS2269 4.1 0.7 1.0
N B:GLY2271 4.2 0.8 1.0
SG B:CYS2268 4.2 0.1 1.0
C B:CYS2270 4.3 0.4 1.0
O B:LYS2274 4.4 0.2 1.0
N B:CYS2275 4.4 0.9 1.0
CB B:CYS2268 4.5 0.6 1.0
CA B:LYS2269 4.5 0.5 1.0
N B:LYS2269 4.5 0.8 1.0
CB B:CYS2220 4.7 0.4 1.0
C B:LYS2274 4.8 0.6 1.0
CA B:CYS2268 4.9 0.2 1.0

Zinc binding site 5 out of 6 in 6ago

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Zinc binding site 5 out of 6 in the Crystal Structure of MRG15-ASH1L Histone Methyltransferase Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Crystal Structure of MRG15-ASH1L Histone Methyltransferase Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn2302

b:95.9
occ:1.00
 SG B:CYS2108 2.3 0.5 1.0
CB B:CYS2091 2.3 0.6 1.0
CB B:CYS2108 2.4 0.3 1.0
SG B:CYS2091 2.5 96.8 1.0
SG B:CYS2104 2.7 0.6 1.0
CB B:CYS2104 3.5 98.0 1.0
ZN B:ZN2303 3.7 98.0 1.0
CA B:CYS2091 3.8 0.9 1.0
SG B:CYS2117 3.8 95.7 1.0
CA B:CYS2108 3.9 0.3 1.0
O B:CYS2091 4.1 0.2 1.0
CB B:ASN2110 4.3 0.6 1.0
C B:CYS2091 4.3 0.7 1.0
SG B:CYS2093 4.4 0.4 1.0
CA B:CYS2104 4.5 0.9 1.0
C B:CYS2108 4.5 0.1 1.0
N B:ASN2110 4.7 0.8 1.0
N B:CYS2091 4.8 0.1 1.0
N B:LEU2109 4.8 0.3 1.0
N B:CYS2108 4.8 0.5 1.0
CB B:CYS2093 4.9 0.8 1.0
ND2 B:ASN2110 4.9 89.7 1.0

Zinc binding site 6 out of 6 in 6ago

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Zinc binding site 6 out of 6 in the Crystal Structure of MRG15-ASH1L Histone Methyltransferase Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Crystal Structure of MRG15-ASH1L Histone Methyltransferase Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn2303

b:98.0
occ:1.00
 SG B:CYS2122 2.3 96.0 1.0
SG B:CYS2117 2.4 95.7 1.0
SG B:CYS2128 2.5 0.6 1.0
SG B:CYS2104 2.8 0.6 1.0
CB B:CYS2117 3.0 87.6 1.0
CB B:CYS2122 3.2 94.9 1.0
SG B:CYS2091 3.6 96.8 1.0
CB B:CYS2128 3.7 97.7 1.0
ZN B:ZN2302 3.7 95.9 1.0
CB B:CYS2104 4.3 98.0 1.0
CA B:CYS2122 4.3 0.1 1.0
CB B:CYS2091 4.4 0.6 1.0
CB B:ASN2130 4.5 0.8 1.0
CA B:CYS2117 4.5 87.1 1.0
NE2 B:GLN2131 4.7 0.9 1.0
CA B:CYS2128 4.8 0.5 1.0
CB B:CYS2124 5.0 0.3 1.0

Reference:

Y.Lee, E.Yoon, S.Cho, S.Schmahling, J.Muller, J.J.Song. Structural Basis of MRG15-Mediated Activation of the ASH1L Histone Methyltransferase By Releasing An Autoinhibitory Loop. Structure V. 27 846 2019.
ISSN: ISSN 0969-2126
PubMed: 30827841
DOI: 10.1016/J.STR.2019.01.016
Page generated: Mon Oct 28 17:31:38 2024

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