Zinc in PDB 5guv: The Crystal Structure of Mouse DNMT1 (731-1602) Mutant - R1279D

All present enzymatic activity of The Crystal Structure of Mouse DNMT1 (731-1602) Mutant - R1279D:
2.1.1.37;

The structure of The Crystal Structure of Mouse DNMT1 (731-1602) Mutant - R1279D, PDB code: 5guv was solved by F.Ye, S.J.Chen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	61.60 / 3.08
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	79.039, 79.039, 393.276, 90.00, 90.00, 90.00
R / Rfree (%)	21.4 / 26.8

The binding sites of Zinc atom in the The Crystal Structure of Mouse DNMT1 (731-1602) Mutant - R1279D (pdb code 5guv). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the The Crystal Structure of Mouse DNMT1 (731-1602) Mutant - R1279D, PDB code: 5guv:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the The Crystal Structure of Mouse DNMT1 (731-1602) Mutant - R1279D


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Crystal Structure of Mouse DNMT1 (731-1602) Mutant - R1279D within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1701 b:62.0 occ:1.00 SG A:CYS1481 2.1 54.7 1.0 SG A:CYS1479 2.3 43.9 1.0 NE2 A:HIS1504 2.4 54.2 1.0 SG A:CYS1487 2.9 56.2 1.0 CB A:CYS1479 3.0 53.3 1.0 CD2 A:HIS1504 3.0 54.2 1.0 CB A:CYS1481 3.1 60.3 1.0 CE1 A:HIS1504 3.5 48.3 1.0 N A:CYS1481 3.8 64.0 1.0 CB A:CYS1487 3.9 67.8 1.0 CA A:CYS1487 4.0 64.1 1.0 CA A:CYS1481 4.1 62.4 1.0 CG A:HIS1504 4.2 44.3 1.0 CA A:CYS1479 4.4 59.5 1.0 ND1 A:HIS1504 4.4 48.4 1.0 C A:CYS1479 4.6 59.5 1.0 N A:SER1480 4.7 60.4 1.0 N A:CYS1487 4.7 64.9 1.0 C A:CYS1481 4.9 61.0 1.0

Zinc binding site 2 out of 2 in the The Crystal Structure of Mouse DNMT1 (731-1602) Mutant - R1279D


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of The Crystal Structure of Mouse DNMT1 (731-1602) Mutant - R1279D within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1702 b:50.9 occ:1.00 NE2 A:HIS796 2.0 46.8 1.0 SG A:CYS900 2.1 35.0 1.0 SG A:CYS823 2.2 48.4 1.0 SG A:CYS897 2.2 41.6 1.0 CE1 A:HIS796 2.9 46.8 1.0 CD2 A:HIS796 2.9 53.7 1.0 CB A:CYS823 3.0 44.6 1.0 CB A:CYS897 3.2 47.2 1.0 CB A:CYS900 3.4 43.5 1.0 N A:CYS900 3.5 43.7 1.0 CA A:CYS900 3.9 46.1 1.0 ND1 A:HIS796 4.0 47.5 1.0 CG A:HIS796 4.0 51.7 1.0 CB A:SER899 4.1 42.2 1.0 CA A:CYS823 4.4 46.6 1.0 C A:SER899 4.5 42.6 1.0 OG A:SER899 4.5 41.1 1.0 CA A:CYS897 4.6 50.6 1.0 C A:CYS823 4.7 52.5 1.0 CA A:SER899 4.8 42.0 1.0 O A:CYS897 4.8 47.8 1.0 C A:CYS897 4.9 42.8 1.0 O A:HOH1826 4.9 45.2 1.0 N A:GLU824 5.0 49.1 1.0 N A:SER899 5.0 35.9 1.0

F.Ye, X.Q.Kong, H.Zhang, Y.Liu, Z.Shao, J.Jin, Y.Cai, R.Zhang, L.Li, Y.W.Zhang, Y.C.Liu, C.Zhang, W.Xie, K.Yu, H.Ding, K.Zhao, S.Chen, H.Jiang, S.B.Baylin, C.Luo. Biochemical Studies and Molecular Dynamic Simulations Reveal the Molecular Basis of Conformational Changes in Dna Methyltransferase-1. Acs Chem. Biol. V. 13 772 2018.
ISSN: ESSN 1554-8937
PubMed: 29381856
DOI: 10.1021/ACSCHEMBIO.7B00890