Iron in PDB 6rq8: CYP121 in Complex with 3-Iodo Dicyclotyrosine

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

The structure of CYP121 in Complex with 3-Iodo Dicyclotyrosine, PDB code: 6rq8 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)	53.47 / 1.41
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	77.770, 77.770, 263.870, 90.00, 90.00, 120.00
R / Rfree (%)	16.1 / 18

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

Iodine

(I)

1 atom

The binding sites of Iron atom in the CYP121 in Complex with 3-Iodo Dicyclotyrosine (pdb code 6rq8). 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-Iodo Dicyclotyrosine, PDB code: 6rq8:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the CYP121 in Complex with 3-Iodo 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-Iodo Dicyclotyrosine within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe402 b:8.3 occ:0.62 FE A:HEM402 0.0 8.3 0.6 FE A:HEM402 0.1 11.5 0.4 ND A:HEM402 2.0 7.8 0.6 ND A:HEM402 2.0 7.0 0.4 NA A:HEM402 2.0 8.4 0.4 NA A:HEM402 2.1 7.2 0.6 NB A:HEM402 2.1 8.0 0.4 NC A:HEM402 2.1 8.3 0.4 NB A:HEM402 2.1 8.1 0.6 NC A:HEM402 2.1 9.0 0.6 SG A:CYS345 2.4 9.7 1.0 C4D A:HEM402 3.0 8.6 0.6 C1D A:HEM402 3.0 9.6 0.6 C4D A:HEM402 3.0 8.4 0.4 C4B A:HEM402 3.0 7.8 0.6 C1D A:HEM402 3.0 8.2 0.4 C1A A:HEM402 3.0 8.8 0.4 C4B A:HEM402 3.0 9.4 0.4 C1B A:HEM402 3.0 9.6 0.4 C4A A:HEM402 3.0 10.1 0.4 C1A A:HEM402 3.0 8.7 0.6 C4C A:HEM402 3.0 9.7 0.6 C4C A:HEM402 3.1 7.8 0.4 C1B A:HEM402 3.1 7.9 0.6 C1C A:HEM402 3.1 8.1 0.4 C1C A:HEM402 3.1 9.6 0.6 C4A A:HEM402 3.1 8.2 0.6 CB A:CYS345 3.4 11.6 1.0 CHC A:HEM402 3.4 9.1 0.6 CHA A:HEM402 3.4 9.2 0.4 CHA A:HEM402 3.4 8.9 0.6 CHC A:HEM402 3.4 9.0 0.4 CHD A:HEM402 3.4 8.9 0.6 CHB A:HEM402 3.4 8.7 0.4 CHD A:HEM402 3.4 8.4 0.4 CHB A:HEM402 3.5 8.3 0.6 CA A:CYS345 4.1 7.5 1.0 C2A A:HEM402 4.2 10.3 0.4 C3A A:HEM402 4.2 11.5 0.4 C3D A:HEM402 4.2 10.4 0.6 C2D A:HEM402 4.2 11.6 0.6 C3C A:HEM402 4.2 9.7 0.6 I25 A:KEH403 4.2 15.5 1.0 C3C A:HEM402 4.2 8.8 0.4 C2B A:HEM402 4.2 9.7 0.4 C3B A:HEM402 4.3 8.8 0.6 C2C A:HEM402 4.3 10.2 0.6 C2A A:HEM402 4.3 8.8 0.6 C2C A:HEM402 4.3 8.6 0.4 C3D A:HEM402 4.3 9.2 0.4 C3B A:HEM402 4.3 11.0 0.4 C2D A:HEM402 4.3 9.0 0.4 C3A A:HEM402 4.3 9.1 0.6 C2B A:HEM402 4.3 8.7 0.6 OG A:SER237 4.6 8.7 1.0 CD A:PRO346 4.7 10.5 1.0 C A:CYS345 4.9 10.1 1.0 CB A:SER237 4.9 8.8 1.0 N A:GLY347 4.9 11.0 1.0 N A:PRO346 5.0 9.3 1.0

Iron binding site 2 out of 2 in the CYP121 in Complex with 3-Iodo 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-Iodo Dicyclotyrosine within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe402 b:11.5 occ:0.38 FE A:HEM402 0.0 11.5 0.4 FE A:HEM402 0.1 8.3 0.6 ND A:HEM402 2.0 7.0 0.4 ND A:HEM402 2.0 7.8 0.6 NA A:HEM402 2.0 8.4 0.4 NA A:HEM402 2.0 7.2 0.6 NC A:HEM402 2.1 8.3 0.4 NB A:HEM402 2.1 8.1 0.6 NB A:HEM402 2.1 8.0 0.4 NC A:HEM402 2.1 9.0 0.6 SG A:CYS345 2.4 9.7 1.0 C4D A:HEM402 3.0 8.6 0.6 C4D A:HEM402 3.0 8.4 0.4 C1D A:HEM402 3.0 9.6 0.6 C1D A:HEM402 3.0 8.2 0.4 C1A A:HEM402 3.0 8.8 0.4 C4B A:HEM402 3.0 7.8 0.6 C1A A:HEM402 3.0 8.7 0.6 C4C A:HEM402 3.0 7.8 0.4 C4B A:HEM402 3.0 9.4 0.4 C4A A:HEM402 3.0 10.1 0.4 C1B A:HEM402 3.1 9.6 0.4 C1B A:HEM402 3.1 7.9 0.6 C4C A:HEM402 3.1 9.7 0.6 C4A A:HEM402 3.1 8.2 0.6 C1C A:HEM402 3.1 8.1 0.4 C1C A:HEM402 3.1 9.6 0.6 CHA A:HEM402 3.4 9.2 0.4 CHA A:HEM402 3.4 8.9 0.6 CHC A:HEM402 3.4 9.1 0.6 CB A:CYS345 3.4 11.6 1.0 CHD A:HEM402 3.4 8.4 0.4 CHD A:HEM402 3.4 8.9 0.6 CHC A:HEM402 3.4 9.0 0.4 CHB A:HEM402 3.4 8.7 0.4 CHB A:HEM402 3.4 8.3 0.6 CA A:CYS345 4.1 7.5 1.0 I25 A:KEH403 4.2 15.5 1.0 C2A A:HEM402 4.2 10.3 0.4 C3D A:HEM402 4.2 10.4 0.6 C3A A:HEM402 4.2 11.5 0.4 C2D A:HEM402 4.2 11.6 0.6 C3C A:HEM402 4.2 8.8 0.4 C2A A:HEM402 4.2 8.8 0.6 C3D A:HEM402 4.2 9.2 0.4 C3C A:HEM402 4.2 9.7 0.6 C2D A:HEM402 4.2 9.0 0.4 C3B A:HEM402 4.2 8.8 0.6 C3A A:HEM402 4.2 9.1 0.6 C2C A:HEM402 4.3 8.6 0.4 C2B A:HEM402 4.3 8.7 0.6 C2B A:HEM402 4.3 9.7 0.4 C2C A:HEM402 4.3 10.2 0.6 C3B A:HEM402 4.3 11.0 0.4 OG A:SER237 4.6 8.7 1.0 CD A:PRO346 4.7 10.5 1.0 CB A:SER237 4.8 8.8 1.0 C A:CYS345 4.9 10.1 1.0 N A:GLY347 5.0 11.0 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