Chlorine in PDB 5vmw: Kaiso (ZBTB33) Zinc Finger Dna Binding Domain in Complex with A Double Cpg-Methylated Dna Resembling the Specific Kaiso Binding Sequence (Kbs)

Protein crystallography data

The structure of Kaiso (ZBTB33) Zinc Finger Dna Binding Domain in Complex with A Double Cpg-Methylated Dna Resembling the Specific Kaiso Binding Sequence (Kbs), PDB code: 5vmw was solved by E.N.Nikolova, R.L.Stanfield, M.A.Martinez-Yamout, H.J.Dyson, P.E.Wright, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.67 / 2.40
Space group C 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 44.341, 184.149, 105.189, 90.00, 90.00, 90.00
R / Rfree (%) 17.7 / 21.7

Other elements in 5vmw:

The structure of Kaiso (ZBTB33) Zinc Finger Dna Binding Domain in Complex with A Double Cpg-Methylated Dna Resembling the Specific Kaiso Binding Sequence (Kbs) also contains other interesting chemical elements:

Zinc (Zn) 3 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Kaiso (ZBTB33) Zinc Finger Dna Binding Domain in Complex with A Double Cpg-Methylated Dna Resembling the Specific Kaiso Binding Sequence (Kbs) (pdb code 5vmw). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Kaiso (ZBTB33) Zinc Finger Dna Binding Domain in Complex with A Double Cpg-Methylated Dna Resembling the Specific Kaiso Binding Sequence (Kbs), PDB code: 5vmw:

Chlorine binding site 1 out of 1 in 5vmw

Go back to Chlorine Binding Sites List in 5vmw
Chlorine binding site 1 out of 1 in the Kaiso (ZBTB33) Zinc Finger Dna Binding Domain in Complex with A Double Cpg-Methylated Dna Resembling the Specific Kaiso Binding Sequence (Kbs)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Kaiso (ZBTB33) Zinc Finger Dna Binding Domain in Complex with A Double Cpg-Methylated Dna Resembling the Specific Kaiso Binding Sequence (Kbs) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl704

b:46.6
occ:0.50
O A:HOH807 3.1 45.8 1.0
N A:ARG548 3.3 43.0 1.0
NH2 A:ARG590 3.6 47.9 1.0
O A:ARG548 3.8 50.4 1.0
CG A:GLU547 4.0 48.2 1.0
CA A:GLU547 4.1 47.4 1.0
CA A:ARG548 4.2 39.8 1.0
C A:GLU547 4.2 44.4 1.0
C A:ARG548 4.3 48.5 1.0
CB A:ARG548 4.4 39.0 1.0
CZ A:ARG590 4.5 40.7 1.0
NE A:ARG590 4.5 50.1 1.0
CB A:GLU547 4.5 51.0 1.0
CG A:ARG548 4.7 43.2 1.0

Reference:

E.N.Nikolova, R.L.Stanfield, H.J.Dyson, P.E.Wright. Ch···O Hydrogen Bonds Mediate Highly Specific Recognition of Methylated Cpg Sites By the Zinc Finger Protein Kaiso. Biochemistry V. 57 2109 2018.
ISSN: ISSN 1520-4995
PubMed: 29546986
DOI: 10.1021/ACS.BIOCHEM.8B00065
Page generated: Sat Dec 12 12:34:36 2020

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