Iron in PDB 6rq9: CYP121 in Complex with O-Methyl Dicyclotyrosine

All present enzymatic activity of CYP121 in Complex with O-Methyl Dicyclotyrosine:
1.14.19.70;

The structure of CYP121 in Complex with O-Methyl Dicyclotyrosine, PDB code: 6rq9 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)	60.03 / 1.40
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	77.830, 77.830, 264.030, 90.00, 90.00, 120.00
R / Rfree (%)	17 / 18.9

The binding sites of Iron atom in the CYP121 in Complex with O-Methyl Dicyclotyrosine (pdb code 6rq9). 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 O-Methyl Dicyclotyrosine, PDB code: 6rq9:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the CYP121 in Complex with O-Methyl 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 O-Methyl Dicyclotyrosine within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe402 b:12.4 occ:0.69 FE A:HEM402 0.0 12.4 0.7 FE A:HEM402 0.0 12.5 0.3 ND A:HEM402 1.9 11.8 0.3 ND A:HEM402 2.0 13.4 0.7 NA A:HEM402 2.0 13.0 0.3 NA A:HEM402 2.0 12.3 0.7 NB A:HEM402 2.1 11.5 0.3 NC A:HEM402 2.1 12.8 0.7 NC A:HEM402 2.1 13.0 0.3 NB A:HEM402 2.1 11.9 0.7 SG A:CYS345 2.4 13.2 1.0 C4D A:HEM402 2.9 14.6 0.7 C4D A:HEM402 2.9 12.3 0.3 C1D A:HEM402 2.9 13.5 0.7 C1A A:HEM402 3.0 14.5 0.3 C1D A:HEM402 3.0 11.3 0.3 C4B A:HEM402 3.0 12.7 0.7 C1A A:HEM402 3.0 12.9 0.7 C4C A:HEM402 3.0 13.8 0.7 C4B A:HEM402 3.0 11.9 0.3 C4A A:HEM402 3.0 12.7 0.3 C1B A:HEM402 3.0 13.3 0.3 C4C A:HEM402 3.1 11.0 0.3 C1B A:HEM402 3.1 10.9 0.7 C4A A:HEM402 3.1 11.0 0.7 C1C A:HEM402 3.1 12.9 0.7 C1C A:HEM402 3.1 12.8 0.3 CHA A:HEM402 3.4 12.1 0.3 CB A:CYS345 3.4 14.8 1.0 CHA A:HEM402 3.4 12.2 0.7 CHD A:HEM402 3.4 12.9 0.7 CHC A:HEM402 3.4 12.1 0.7 CHD A:HEM402 3.4 11.9 0.3 CHB A:HEM402 3.4 11.6 0.3 CHC A:HEM402 3.4 12.3 0.3 CHB A:HEM402 3.5 11.7 0.7 CAY A:KEQ403 3.9 18.3 1.0 CA A:CYS345 4.1 12.0 1.0 C2A A:HEM402 4.2 15.6 0.3 C3D A:HEM402 4.2 15.3 0.7 C2D A:HEM402 4.2 15.5 0.7 C3A A:HEM402 4.2 14.8 0.3 C3C A:HEM402 4.2 12.3 0.7 C3D A:HEM402 4.2 13.3 0.3 C2D A:HEM402 4.2 13.4 0.3 C2A A:HEM402 4.2 13.3 0.7 C2C A:HEM402 4.2 13.6 0.7 C3A A:HEM402 4.2 13.3 0.7 C2B A:HEM402 4.2 12.7 0.3 C3C A:HEM402 4.2 13.2 0.3 C3B A:HEM402 4.3 12.2 0.7 C3B A:HEM402 4.3 13.9 0.3 C2B A:HEM402 4.3 13.1 0.7 C2C A:HEM402 4.3 12.4 0.3 CD A:PRO346 4.7 14.2 1.0 OG A:SER237 4.8 12.5 1.0 C A:CYS345 4.9 13.2 1.0 CB A:SER237 4.9 12.2 1.0 N A:GLY347 5.0 13.8 1.0 N A:PRO346 5.0 13.7 1.0

Iron binding site 2 out of 2 in the CYP121 in Complex with O-Methyl 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 O-Methyl Dicyclotyrosine within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe402 b:12.5 occ:0.31 FE A:HEM402 0.0 12.5 0.3 FE A:HEM402 0.0 12.4 0.7 ND A:HEM402 1.9 11.8 0.3 ND A:HEM402 2.0 13.4 0.7 NA A:HEM402 2.0 12.3 0.7 NA A:HEM402 2.0 13.0 0.3 NC A:HEM402 2.1 13.0 0.3 NB A:HEM402 2.1 11.9 0.7 NB A:HEM402 2.1 11.5 0.3 NC A:HEM402 2.1 12.8 0.7 SG A:CYS345 2.4 13.2 1.0 C4D A:HEM402 2.9 12.3 0.3 C4D A:HEM402 2.9 14.6 0.7 C1D A:HEM402 2.9 11.3 0.3 C1D A:HEM402 3.0 13.5 0.7 C1A A:HEM402 3.0 14.5 0.3 C1A A:HEM402 3.0 12.9 0.7 C4B A:HEM402 3.0 12.7 0.7 C4C A:HEM402 3.0 11.0 0.3 C4C A:HEM402 3.0 13.8 0.7 C4A A:HEM402 3.0 11.0 0.7 C4B A:HEM402 3.0 11.9 0.3 C4A A:HEM402 3.0 12.7 0.3 C1B A:HEM402 3.0 10.9 0.7 C1B A:HEM402 3.1 13.3 0.3 C1C A:HEM402 3.1 12.9 0.7 C1C A:HEM402 3.1 12.8 0.3 CHA A:HEM402 3.3 12.1 0.3 CHA A:HEM402 3.4 12.2 0.7 CB A:CYS345 3.4 14.8 1.0 CHD A:HEM402 3.4 11.9 0.3 CHD A:HEM402 3.4 12.9 0.7 CHC A:HEM402 3.4 12.1 0.7 CHB A:HEM402 3.4 11.7 0.7 CHC A:HEM402 3.4 12.3 0.3 CHB A:HEM402 3.5 11.6 0.3 CAY A:KEQ403 3.9 18.3 1.0 CA A:CYS345 4.1 12.0 1.0 C2A A:HEM402 4.2 15.6 0.3 C3D A:HEM402 4.2 13.3 0.3 C3D A:HEM402 4.2 15.3 0.7 C2D A:HEM402 4.2 13.4 0.3 C2A A:HEM402 4.2 13.3 0.7 C2D A:HEM402 4.2 15.5 0.7 C3A A:HEM402 4.2 14.8 0.3 C3A A:HEM402 4.2 13.3 0.7 C3C A:HEM402 4.2 12.3 0.7 C3C A:HEM402 4.2 13.2 0.3 C3B A:HEM402 4.2 12.2 0.7 C2B A:HEM402 4.2 13.1 0.7 C2C A:HEM402 4.3 13.6 0.7 C2C A:HEM402 4.3 12.4 0.3 C2B A:HEM402 4.3 12.7 0.3 C3B A:HEM402 4.3 13.9 0.3 CD A:PRO346 4.7 14.2 1.0 OG A:SER237 4.7 12.5 1.0 C A:CYS345 4.9 13.2 1.0 CB A:SER237 4.9 12.2 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