Zinc in PDB 3pt9: Crystal Structure of Mouse DNMT1(731-1602) in the Free State

All present enzymatic activity of Crystal Structure of Mouse DNMT1(731-1602) in the Free State:
2.1.1.37;

The structure of Crystal Structure of Mouse DNMT1(731-1602) in the Free State, PDB code: 3pt9 was solved by J.Song, D.J.Patel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.88 / 2.50
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	75.567, 79.685, 162.650, 90.00, 90.00, 90.00
R / Rfree (%)	19.6 / 25.6

The binding sites of Zinc atom in the Crystal Structure of Mouse DNMT1(731-1602) in the Free State (pdb code 3pt9). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Mouse DNMT1(731-1602) in the Free State, PDB code: 3pt9:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Mouse DNMT1(731-1602) in the Free State


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 Mouse DNMT1(731-1602) in the Free State within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1 b:48.7 occ:1.00 SG A:CYS1481 2.3 44.9 1.0 SG A:CYS1479 2.3 42.0 1.0 SG A:CYS1487 2.3 37.6 1.0 NE2 A:HIS1504 2.5 40.5 1.0 CD2 A:HIS1504 3.1 39.4 1.0 CB A:CYS1479 3.2 39.7 1.0 CB A:CYS1481 3.2 43.2 1.0 O A:HOH208 3.3 46.6 1.0 CB A:CYS1487 3.4 36.7 1.0 CE1 A:HIS1504 3.6 40.8 1.0 CA A:CYS1487 3.9 38.7 1.0 N A:CYS1481 4.0 40.8 1.0 CA A:CYS1481 4.2 41.6 1.0 CG A:HIS1504 4.4 38.7 1.0 CA A:CYS1479 4.6 39.9 1.0 ND1 A:HIS1504 4.6 40.5 1.0 N A:CYS1487 4.7 38.9 1.0 C A:CYS1479 4.8 41.1 1.0 N A:SER1480 4.8 40.0 1.0 O A:HOH217 4.9 43.5 1.0 C A:CYS1487 5.0 40.8 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Mouse DNMT1(731-1602) in the Free State


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 Mouse DNMT1(731-1602) in the Free State within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn2 b:45.3 occ:1.00 NE2 A:HIS796 2.0 35.6 1.0 SG A:CYS900 2.1 37.0 1.0 SG A:CYS897 2.3 36.1 1.0 SG A:CYS823 2.3 29.8 1.0 CB A:CYS823 3.0 33.2 1.0 CE1 A:HIS796 3.0 34.5 1.0 CD2 A:HIS796 3.0 33.6 1.0 CB A:CYS900 3.3 33.9 1.0 CB A:CYS897 3.4 34.2 1.0 N A:CYS900 3.5 33.6 1.0 CA A:CYS900 3.8 34.1 1.0 CB A:SER899 4.1 33.1 1.0 ND1 A:HIS796 4.1 33.5 1.0 CG A:HIS796 4.2 35.3 1.0 C A:SER899 4.4 35.7 1.0 CA A:CYS823 4.4 32.6 1.0 OG A:SER899 4.4 28.5 1.0 CA A:SER899 4.7 32.9 1.0 C A:CYS823 4.8 33.0 1.0 CA A:CYS897 4.8 33.4 1.0 O A:CYS897 4.8 29.8 1.0

J.Song, O.Rechkoblit, T.H.Bestor, D.J.Patel. Structure of DNMT1-Dna Complex Reveals A Role For Autoinhibition in Maintenance Dna Methylation. Science V. 331 1036 2011.
ISSN: ISSN 0036-8075
PubMed: 21163962
DOI: 10.1126/SCIENCE.1195380