Zinc in PDB 4cwx: Alpha-Ketoglutarate-Dependent Dioxygenase COMPLEX1

All present enzymatic activity of Alpha-Ketoglutarate-Dependent Dioxygenase COMPLEX1:
1.14.13.39;

The structure of Alpha-Ketoglutarate-Dependent Dioxygenase COMPLEX1, PDB code: 4cwx was solved by H.Li, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.70 / 2.15
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	57.942, 106.494, 156.981, 90.00, 90.00, 90.00
R / Rfree (%)	17.052 / 20.984

The structure of Alpha-Ketoglutarate-Dependent Dioxygenase COMPLEX1 also contains other interesting chemical elements:

Arsenic	(As)	2 atoms
Iron	(Fe)	2 atoms

The binding sites of Zinc atom in the Alpha-Ketoglutarate-Dependent Dioxygenase COMPLEX1 (pdb code 4cwx). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Alpha-Ketoglutarate-Dependent Dioxygenase COMPLEX1, PDB code: 4cwx:

Zinc binding site 1 out of 1 in the Alpha-Ketoglutarate-Dependent Dioxygenase COMPLEX1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Alpha-Ketoglutarate-Dependent Dioxygenase COMPLEX1 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1483 b:61.9 occ:1.00 SG B:CYS101 2.5 60.2 1.0 SG A:CYS96 2.5 56.8 1.0 SG B:CYS96 2.5 61.1 1.0 SG A:CYS101 2.6 64.5 1.0 CB B:CYS101 3.2 60.0 1.0 CB A:CYS101 3.4 63.3 1.0 CB B:CYS96 3.5 61.9 1.0 CB A:CYS96 3.6 64.8 1.0 CA B:CYS101 3.7 62.5 1.0 CA A:CYS101 3.8 67.0 1.0 N B:GLY103 4.0 64.1 1.0 N B:LEU102 4.1 63.7 1.0 N A:GLY103 4.2 69.3 1.0 C B:CYS101 4.2 61.5 1.0 N A:LEU102 4.3 69.3 1.0 CA B:GLY103 4.4 60.6 1.0 CA A:GLY103 4.4 64.7 1.0 C A:CYS101 4.4 68.6 1.0 CA B:CYS96 4.9 65.3 1.0 CA A:CYS96 4.9 70.4 1.0 C B:LEU102 4.9 63.9 1.0 N B:CYS101 5.0 62.2 1.0

H.Li, J.Jamal, S.L.Delker, C.Plaza, H.Ji, Q.Jing, H.Huang, S.Kang, R.B.Silverman, T.L.Poulos. Mobility of A Conserved Tyrosine Residue Controls Isoform- Dependent Enzyme-Inhibitor Interactions in Nitric Oxide Synthases. Biochemistry V. 53 5272 2014.
ISSN: ISSN 0006-2960
PubMed: 25089924
DOI: 10.1021/BI500561H