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Fluorine in PDB 7ubu: Crystal Structure of ZMET2 in Complex with Hemimethylated Cag Dna and A Histone H3KC9ME2 Peptide

Enzymatic activity of Crystal Structure of ZMET2 in Complex with Hemimethylated Cag Dna and A Histone H3KC9ME2 Peptide

All present enzymatic activity of Crystal Structure of ZMET2 in Complex with Hemimethylated Cag Dna and A Histone H3KC9ME2 Peptide:
2.1.1.37;

Protein crystallography data

The structure of Crystal Structure of ZMET2 in Complex with Hemimethylated Cag Dna and A Histone H3KC9ME2 Peptide, PDB code: 7ubu was solved by J.Fang, J.Song, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 96.81 / 2.39
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 64.574, 121.392, 160.446, 90, 90, 90
R / Rfree (%) 21.1 / 25.6

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Crystal Structure of ZMET2 in Complex with Hemimethylated Cag Dna and A Histone H3KC9ME2 Peptide (pdb code 7ubu). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total only one binding site of Fluorine was determined in the Crystal Structure of ZMET2 in Complex with Hemimethylated Cag Dna and A Histone H3KC9ME2 Peptide, PDB code: 7ubu:

Fluorine binding site 1 out of 1 in 7ubu

Go back to Fluorine Binding Sites List in 7ubu
Fluorine binding site 1 out of 1 in the Crystal Structure of ZMET2 in Complex with Hemimethylated Cag Dna and A Histone H3KC9ME2 Peptide


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of ZMET2 in Complex with Hemimethylated Cag Dna and A Histone H3KC9ME2 Peptide within 5.0Å range:
probe atom residue distance (Å) B Occ
C:F10

b:82.8
occ:1.00
 F C:C4910 0.0 82.8 1.0
C5 C:C4910 1.3 72.5 1.0
C4 C:C4910 2.3 74.2 1.0
CM5 C:C4910 2.3 69.6 1.0
C6 C:C4910 2.4 70.2 1.0
SG A:CYS517 2.4 69.8 1.0
N A:CYS517 2.5 66.1 1.0
CB A:CYS517 2.5 69.6 1.0
N4 C:C4910 2.7 73.8 1.0
CA A:CYS517 3.0 60.8 1.0
O A:PRO515 3.1 66.9 1.0
C A:PRO516 3.2 62.0 1.0
N3 C:C4910 3.5 71.0 1.0
N1 C:C4910 3.6 67.1 1.0
CA A:PRO516 3.7 65.1 1.0
OD1 A:ASN560 3.9 64.9 1.0
C2 C:C4910 4.0 69.5 1.0
O A:PRO516 4.0 67.1 1.0
C A:PRO515 4.1 60.1 1.0
C A:CYS517 4.2 64.2 1.0
ND2 A:ASN560 4.3 64.3 1.0
CG A:ASN560 4.3 71.0 1.0
OE1 A:GLN518 4.3 65.9 1.0
N A:PRO516 4.4 60.5 1.0
O A:GLY514 4.5 63.7 1.0
N A:GLN518 4.6 61.4 1.0
CG1 A:VAL561 4.7 61.0 1.0
C1' C:C4910 4.8 69.0 1.0
CD A:GLN518 5.0 67.9 1.0

Reference:

J.Fang, J.Jiang, S.M.Leichter, J.Liu, M.Biswal, N.Khudaverdyan, X.Zhong, J.Song. Mechanistic Basis For Maintenance of Chg Dna Methylation in Plants. Nat Commun V. 13 3877 2022.
ISSN: ESSN 2041-1723
PubMed: 35790763
DOI: 10.1038/S41467-022-31627-3
Page generated: Wed Jul 16 00:55:57 2025

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