Iron 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
Zinc	(Zn)	1 atom

The binding sites of Iron atom in the Alpha-Ketoglutarate-Dependent Dioxygenase COMPLEX1 (pdb code 4cwx). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Alpha-Ketoglutarate-Dependent Dioxygenase COMPLEX1, PDB code: 4cwx:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Alpha-Ketoglutarate-Dependent Dioxygenase COMPLEX1


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Alpha-Ketoglutarate-Dependent Dioxygenase COMPLEX1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe500 b:32.6 occ:1.00 FE A:HEM500 0.0 32.6 1.0 NC A:HEM500 2.0 30.7 1.0 NA A:HEM500 2.0 32.9 1.0 ND A:HEM500 2.1 30.6 1.0 NB A:HEM500 2.1 29.2 1.0 SG A:CYS186 2.4 34.9 1.0 C4C A:HEM500 3.0 32.3 1.0 C1D A:HEM500 3.1 33.0 1.0 C1A A:HEM500 3.1 30.1 1.0 C4A A:HEM500 3.1 31.1 1.0 C1C A:HEM500 3.1 28.5 1.0 C1B A:HEM500 3.1 30.5 1.0 C4D A:HEM500 3.1 32.8 1.0 C4B A:HEM500 3.2 31.0 1.0 CB A:CYS186 3.3 34.0 1.0 CHD A:HEM500 3.4 32.2 1.0 CHB A:HEM500 3.5 31.8 1.0 CHA A:HEM500 3.5 32.0 1.0 CHC A:HEM500 3.6 30.7 1.0 C23 A:HW0800 3.9 37.5 1.0 CA A:CYS186 4.1 33.0 1.0 C24 A:HW0800 4.1 38.7 1.0 C3C A:HEM500 4.3 30.5 1.0 NE1 A:TRP180 4.3 31.8 1.0 C2A A:HEM500 4.4 32.9 1.0 C2C A:HEM500 4.4 30.6 1.0 C3A A:HEM500 4.4 32.7 1.0 C2D A:HEM500 4.4 32.8 1.0 C3D A:HEM500 4.4 32.9 1.0 C3B A:HEM500 4.5 30.7 1.0 C22 A:HW0800 4.5 37.1 1.0 C2B A:HEM500 4.5 30.6 1.0 C25 A:HW0800 4.7 41.6 1.0 N A:GLY188 4.7 33.9 1.0 C A:CYS186 4.8 34.2 1.0 N A:VAL187 4.9 32.9 1.0 CD1 A:TRP180 5.0 31.6 1.0 N21 A:HW0800 5.0 38.6 1.0

Iron binding site 2 out of 2 in the Alpha-Ketoglutarate-Dependent Dioxygenase COMPLEX1


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Alpha-Ketoglutarate-Dependent Dioxygenase COMPLEX1 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe500 b:35.2 occ:1.00 FE B:HEM500 0.0 35.2 1.0 NC B:HEM500 2.0 32.5 1.0 NA B:HEM500 2.0 37.8 1.0 ND B:HEM500 2.1 34.7 1.0 NB B:HEM500 2.1 34.7 1.0 SG B:CYS186 2.3 33.6 1.0 C4C B:HEM500 3.1 32.3 1.0 C1C B:HEM500 3.1 32.0 1.0 C4A B:HEM500 3.1 34.9 1.0 C1D B:HEM500 3.1 36.4 1.0 C4B B:HEM500 3.1 35.9 1.0 C1A B:HEM500 3.1 35.6 1.0 C1B B:HEM500 3.1 36.1 1.0 C4D B:HEM500 3.2 36.0 1.0 CB B:CYS186 3.3 33.1 1.0 CHD B:HEM500 3.4 33.6 1.0 CHB B:HEM500 3.5 35.9 1.0 CHC B:HEM500 3.5 33.8 1.0 CHA B:HEM500 3.6 33.7 1.0 C23 B:HW0800 3.8 42.1 1.0 C24 B:HW0800 3.9 41.4 1.0 CA B:CYS186 4.1 34.4 1.0 C3C B:HEM500 4.3 33.7 1.0 NE1 B:TRP180 4.3 38.9 1.0 C2C B:HEM500 4.4 34.5 1.0 C3A B:HEM500 4.4 38.0 1.0 C2A B:HEM500 4.4 38.4 1.0 C3B B:HEM500 4.4 35.5 1.0 C22 B:HW0800 4.4 40.8 1.0 C2D B:HEM500 4.5 36.5 1.0 C2B B:HEM500 4.5 35.2 1.0 C3D B:HEM500 4.5 36.3 1.0 C25 B:HW0800 4.7 43.3 1.0 N B:GLY188 4.7 33.6 1.0 C B:CYS186 4.8 32.6 1.0 N B:VAL187 4.9 33.5 1.0 N22 B:HW0800 5.0 39.4 1.0 CD1 B:TRP180 5.0 37.5 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