Chlorine in PDB 3avs: Catalytic Fragment of Utx/KDM6A Bound with N-Oxyalylglycine, and Ni(II)

The structure of Catalytic Fragment of Utx/KDM6A Bound with N-Oxyalylglycine, and Ni(II), PDB code: 3avs was solved by T.Sengoku, S.Yokoyama, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.07 / 1.85
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	78.872, 82.879, 92.923, 90.00, 90.00, 90.00
R / Rfree (%)	18.3 / 21.8

The structure of Catalytic Fragment of Utx/KDM6A Bound with N-Oxyalylglycine, and Ni(II) also contains other interesting chemical elements:

Zinc	(Zn)	1 atom
Nickel	(Ni)	3 atoms

The binding sites of Chlorine atom in the Catalytic Fragment of Utx/KDM6A Bound with N-Oxyalylglycine, and Ni(II) (pdb code 3avs). 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 Catalytic Fragment of Utx/KDM6A Bound with N-Oxyalylglycine, and Ni(II), PDB code: 3avs:

Chlorine binding site 1 out of 1 in the Catalytic Fragment of Utx/KDM6A Bound with N-Oxyalylglycine, and Ni(II)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Catalytic Fragment of Utx/KDM6A Bound with N-Oxyalylglycine, and Ni(II) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1506 b:69.4 occ:1.00 HE A:ARG1027 2.7 53.7 1.0 HH21 A:ARG1027 2.8 58.6 1.0 HB3 A:ARG1027 3.4 43.2 1.0 NE A:ARG1027 3.5 44.8 1.0 NH2 A:ARG1027 3.6 48.9 1.0 CZ A:ARG1027 4.0 36.5 1.0 O A:HOH328 4.2 53.0 1.0 O A:ARG1027 4.3 34.5 1.0 HH22 A:ARG1027 4.3 58.6 1.0 CB A:ARG1027 4.4 36.0 1.0 O A:HOH133 4.4 47.2 1.0 HG2 A:ARG1027 4.5 37.7 1.0 CD A:ARG1027 4.6 43.1 1.0 CG A:ARG1027 4.7 31.5 1.0 HD3 A:ARG1027 4.8 51.7 1.0 HB2 A:ARG1027 4.9 43.2 1.0 H A:ARG1027 4.9 38.1 1.0 C A:ARG1027 4.9 42.0 1.0

T.Sengoku, S.Yokoyama. Structural Basis For Histone H3 Lys 27 Demethylation By Utx/KDM6A Genes Dev. V. 25 2266 2011.
ISSN: ISSN 0890-9369
PubMed: 22002947
DOI: 10.1101/GAD.172296.111