Iron in PDB 6rq6: CYP121 in Complex with 3-Fluoro Dicyclotyrosine

All present enzymatic activity of CYP121 in Complex with 3-Fluoro Dicyclotyrosine:
1.14.19.70;

The structure of CYP121 in Complex with 3-Fluoro Dicyclotyrosine, PDB code: 6rq6 was solved by H.Poddar, C.Levy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	53.54 / 1.42
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	77.890, 77.890, 264.020, 90.00, 90.00, 120.00
R / Rfree (%)	17.2 / 19.1

The structure of CYP121 in Complex with 3-Fluoro Dicyclotyrosine also contains other interesting chemical elements:

Fluorine

(F)

2 atoms

The binding sites of Iron atom in the CYP121 in Complex with 3-Fluoro Dicyclotyrosine (pdb code 6rq6). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the CYP121 in Complex with 3-Fluoro Dicyclotyrosine, PDB code: 6rq6:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the CYP121 in Complex with 3-Fluoro Dicyclotyrosine


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of CYP121 in Complex with 3-Fluoro Dicyclotyrosine within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe402 b:9.9 occ:0.59 FE A:HEM402 0.0 9.9 0.6 FE A:HEM402 0.0 11.0 0.4 ND A:HEM402 2.0 8.7 0.4 ND A:HEM402 2.0 9.9 0.6 NA A:HEM402 2.0 9.9 0.4 NA A:HEM402 2.0 8.6 0.6 NB A:HEM402 2.1 8.2 0.4 NC A:HEM402 2.1 8.7 0.4 NC A:HEM402 2.1 9.2 0.6 NB A:HEM402 2.1 7.6 0.6 SG A:CYS345 2.3 10.9 1.0 O A:HOH695 2.4 19.9 1.0 C4D A:HEM402 2.9 8.9 0.4 C4D A:HEM402 3.0 10.1 0.6 C1D A:HEM402 3.0 10.7 0.6 C1D A:HEM402 3.0 7.8 0.4 C1A A:HEM402 3.0 10.8 0.4 C1A A:HEM402 3.0 8.9 0.6 C4B A:HEM402 3.0 8.6 0.4 C4B A:HEM402 3.0 7.8 0.6 C4C A:HEM402 3.0 9.8 0.4 C1B A:HEM402 3.1 8.8 0.4 C4A A:HEM402 3.1 10.9 0.4 C4C A:HEM402 3.1 9.4 0.6 C1B A:HEM402 3.1 9.9 0.6 C4A A:HEM402 3.1 7.4 0.6 C1C A:HEM402 3.1 8.6 0.6 C1C A:HEM402 3.1 7.9 0.4 CHA A:HEM402 3.4 11.2 0.4 CHA A:HEM402 3.4 10.8 0.6 CB A:CYS345 3.4 13.0 1.0 CHD A:HEM402 3.4 9.5 0.4 CHD A:HEM402 3.4 10.4 0.6 CHC A:HEM402 3.4 10.3 0.6 CHB A:HEM402 3.4 10.6 0.4 CHC A:HEM402 3.4 10.8 0.4 CHB A:HEM402 3.5 9.4 0.6 CA A:CYS345 4.2 8.8 1.0 C2A A:HEM402 4.2 10.3 0.6 C3D A:HEM402 4.2 10.4 0.4 C2D A:HEM402 4.2 9.6 0.4 C2A A:HEM402 4.2 12.1 0.4 C2D A:HEM402 4.2 12.6 0.6 C3C A:HEM402 4.2 10.5 0.6 C3A A:HEM402 4.2 13.2 0.4 C3A A:HEM402 4.2 9.3 0.6 C3D A:HEM402 4.2 12.4 0.6 C3C A:HEM402 4.2 10.6 0.4 C2C A:HEM402 4.2 10.6 0.6 C2B A:HEM402 4.3 9.9 0.4 C3B A:HEM402 4.3 11.5 0.4 C2C A:HEM402 4.3 9.4 0.4 C3B A:HEM402 4.3 9.2 0.6 C2B A:HEM402 4.3 10.3 0.6 OG A:SER237 4.5 10.5 1.0 CD A:PRO346 4.7 9.8 1.0 CB A:SER237 4.9 9.7 1.0 C A:CYS345 4.9 10.1 1.0 N A:GLY347 5.0 10.7 1.0

Iron binding site 2 out of 2 in the CYP121 in Complex with 3-Fluoro Dicyclotyrosine


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of CYP121 in Complex with 3-Fluoro Dicyclotyrosine within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe402 b:11.0 occ:0.41 FE A:HEM402 0.0 11.0 0.4 FE A:HEM402 0.0 9.9 0.6 ND A:HEM402 1.9 8.7 0.4 ND A:HEM402 2.0 9.9 0.6 NA A:HEM402 2.0 8.6 0.6 NA A:HEM402 2.0 9.9 0.4 NC A:HEM402 2.1 8.7 0.4 NB A:HEM402 2.1 7.6 0.6 NB A:HEM402 2.1 8.2 0.4 NC A:HEM402 2.1 9.2 0.6 SG A:CYS345 2.3 10.9 1.0 O A:HOH695 2.4 19.9 1.0 C4D A:HEM402 2.9 8.9 0.4 C4D A:HEM402 3.0 10.1 0.6 C1D A:HEM402 3.0 7.8 0.4 C1D A:HEM402 3.0 10.7 0.6 C1A A:HEM402 3.0 8.9 0.6 C1A A:HEM402 3.0 10.8 0.4 C4B A:HEM402 3.0 7.8 0.6 C4C A:HEM402 3.0 9.8 0.4 C4B A:HEM402 3.0 8.6 0.4 C4A A:HEM402 3.1 7.4 0.6 C1B A:HEM402 3.1 9.9 0.6 C4A A:HEM402 3.1 10.9 0.4 C1B A:HEM402 3.1 8.8 0.4 C4C A:HEM402 3.1 9.4 0.6 C1C A:HEM402 3.1 8.6 0.6 C1C A:HEM402 3.1 7.9 0.4 CHA A:HEM402 3.4 11.2 0.4 CHA A:HEM402 3.4 10.8 0.6 CB A:CYS345 3.4 13.0 1.0 CHD A:HEM402 3.4 9.5 0.4 CHD A:HEM402 3.4 10.4 0.6 CHC A:HEM402 3.4 10.3 0.6 CHB A:HEM402 3.4 9.4 0.6 CHC A:HEM402 3.4 10.8 0.4 CHB A:HEM402 3.5 10.6 0.4 CA A:CYS345 4.2 8.8 1.0 C2A A:HEM402 4.2 10.3 0.6 C3D A:HEM402 4.2 10.4 0.4 C2D A:HEM402 4.2 9.6 0.4 C3A A:HEM402 4.2 9.3 0.6 C2A A:HEM402 4.2 12.1 0.4 C2D A:HEM402 4.2 12.6 0.6 C3A A:HEM402 4.2 13.2 0.4 C3C A:HEM402 4.2 10.6 0.4 C3C A:HEM402 4.2 10.5 0.6 C3D A:HEM402 4.2 12.4 0.6 C2C A:HEM402 4.3 10.6 0.6 C2B A:HEM402 4.3 9.9 0.4 C2C A:HEM402 4.3 9.4 0.4 C2B A:HEM402 4.3 10.3 0.6 C3B A:HEM402 4.3 11.5 0.4 C3B A:HEM402 4.3 9.2 0.6 OG A:SER237 4.5 10.5 1.0 CD A:PRO346 4.8 9.8 1.0 CB A:SER237 4.9 9.7 1.0 C A:CYS345 4.9 10.1 1.0 N A:GLY347 5.0 10.7 1.0

S.Rajput, K.J.Mclean, H.Poddar, I.R.Selvam, G.Nagalingam, J.A.Triccas, C.W.Levy, A.W.Munro, C.A.Hutton. Structure-Activity Relationships Ofcyclo(L-Tyrosyl-L-Tyrosine) Derivatives Binding Tomycobacterium TUBERCULOSISCYP121: Iodinated Analogues Promote Shift to High-Spin Adduct. J.Med.Chem. V. 62 9792 2019.
ISSN: ISSN 0022-2623
PubMed: 31618032
DOI: 10.1021/ACS.JMEDCHEM.9B01199