Iron in PDB 6rq5: CYP121 in Complex with 3,5-Dimethyl Dicyclotyrosine

All present enzymatic activity of CYP121 in Complex with 3,5-Dimethyl Dicyclotyrosine:
1.14.19.70;

The structure of CYP121 in Complex with 3,5-Dimethyl Dicyclotyrosine, PDB code: 6rq5 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)	66.43 / 1.55
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	76.710, 76.710, 262.300, 90.00, 90.00, 120.00
R / Rfree (%)	17.6 / 20.3

The binding sites of Iron atom in the CYP121 in Complex with 3,5-Dimethyl Dicyclotyrosine (pdb code 6rq5). 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 3,5-Dimethyl Dicyclotyrosine, PDB code: 6rq5:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the CYP121 in Complex with 3,5-Dimethyl 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 3,5-Dimethyl Dicyclotyrosine within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe403 b:9.4 occ:0.69 FE A:HEM403 0.0 9.4 0.7 FE A:HEM403 0.1 8.0 0.3 ND A:HEM403 1.9 9.2 0.3 ND A:HEM403 2.0 7.6 0.7 NA A:HEM403 2.0 7.7 0.3 NA A:HEM403 2.0 9.2 0.7 NC A:HEM403 2.1 8.1 0.3 NC A:HEM403 2.1 7.7 0.7 NB A:HEM403 2.1 8.1 0.7 NB A:HEM403 2.2 7.8 0.3 SG A:CYS345 2.3 10.4 1.0 O A:HOH623 2.4 22.3 1.0 C4D A:HEM403 2.9 9.8 0.7 C4D A:HEM403 2.9 9.1 0.3 C1D A:HEM403 2.9 9.1 0.7 C1D A:HEM403 2.9 7.6 0.3 C1A A:HEM403 3.0 9.8 0.3 C4B A:HEM403 3.0 8.6 0.7 C4C A:HEM403 3.0 8.8 0.7 C1A A:HEM403 3.0 9.1 0.7 C4C A:HEM403 3.0 7.1 0.3 C4A A:HEM403 3.0 7.5 0.7 C4B A:HEM403 3.0 9.2 0.3 C4A A:HEM403 3.0 9.1 0.3 C1C A:HEM403 3.0 9.1 0.7 C1B A:HEM403 3.1 7.0 0.7 C1C A:HEM403 3.1 8.6 0.3 C1B A:HEM403 3.1 8.8 0.3 CHA A:HEM403 3.3 10.2 0.3 CB A:CYS345 3.4 11.2 1.0 CHA A:HEM403 3.4 10.3 0.7 CHD A:HEM403 3.4 9.4 0.3 CHD A:HEM403 3.4 9.5 0.7 CHC A:HEM403 3.4 8.4 0.7 CHB A:HEM403 3.4 9.5 0.7 CHC A:HEM403 3.4 8.4 0.3 CHB A:HEM403 3.5 9.5 0.3 CA A:CYS345 4.1 6.5 1.0 C2A A:HEM403 4.2 11.4 0.3 C3C A:HEM403 4.2 10.3 0.7 C3D A:HEM403 4.2 11.4 0.7 C2D A:HEM403 4.2 11.1 0.7 C2D A:HEM403 4.2 8.9 0.3 C3D A:HEM403 4.2 9.1 0.3 C2C A:HEM403 4.2 11.2 0.7 C3A A:HEM403 4.2 11.0 0.3 C3A A:HEM403 4.2 8.9 0.7 C3C A:HEM403 4.2 7.7 0.3 C2A A:HEM403 4.2 9.1 0.7 C3B A:HEM403 4.2 8.7 0.7 C2B A:HEM403 4.2 7.6 0.7 C2C A:HEM403 4.2 8.7 0.3 C3B A:HEM403 4.3 11.1 0.3 C2B A:HEM403 4.3 10.2 0.3 OG A:SER237 4.6 10.0 1.0 C24 A:KEB402 4.7 14.9 0.6 CD A:PRO346 4.8 10.8 1.0 CB A:SER237 4.8 9.5 1.0 C A:CYS345 4.9 11.1 1.0 N A:GLY347 4.9 9.9 1.0

Iron binding site 2 out of 2 in the CYP121 in Complex with 3,5-Dimethyl 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 3,5-Dimethyl Dicyclotyrosine within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe403 b:8.0 occ:0.31 FE A:HEM403 0.0 8.0 0.3 FE A:HEM403 0.1 9.4 0.7 ND A:HEM403 1.9 9.2 0.3 ND A:HEM403 2.0 7.6 0.7 NA A:HEM403 2.0 7.7 0.3 NA A:HEM403 2.0 9.2 0.7 NC A:HEM403 2.1 8.1 0.3 NC A:HEM403 2.1 7.7 0.7 NB A:HEM403 2.1 8.1 0.7 NB A:HEM403 2.2 7.8 0.3 O A:HOH623 2.3 22.3 1.0 SG A:CYS345 2.4 10.4 1.0 C4D A:HEM403 2.9 9.8 0.7 C4D A:HEM403 2.9 9.1 0.3 C1D A:HEM403 2.9 9.1 0.7 C1D A:HEM403 2.9 7.6 0.3 C1A A:HEM403 3.0 9.8 0.3 C4C A:HEM403 3.0 8.8 0.7 C4B A:HEM403 3.0 8.6 0.7 C4C A:HEM403 3.0 7.1 0.3 C1A A:HEM403 3.0 9.1 0.7 C4A A:HEM403 3.0 7.5 0.7 C4B A:HEM403 3.0 9.2 0.3 C4A A:HEM403 3.0 9.1 0.3 C1C A:HEM403 3.0 9.1 0.7 C1B A:HEM403 3.0 7.0 0.7 C1C A:HEM403 3.1 8.6 0.3 C1B A:HEM403 3.1 8.8 0.3 CHA A:HEM403 3.4 10.2 0.3 CHA A:HEM403 3.4 10.3 0.7 CHD A:HEM403 3.4 9.4 0.3 CHD A:HEM403 3.4 9.5 0.7 CB A:CYS345 3.4 11.2 1.0 CHC A:HEM403 3.4 8.4 0.7 CHB A:HEM403 3.4 9.5 0.7 CHC A:HEM403 3.4 8.4 0.3 CHB A:HEM403 3.5 9.5 0.3 C2A A:HEM403 4.1 11.4 0.3 C3C A:HEM403 4.2 10.3 0.7 C3D A:HEM403 4.2 11.4 0.7 C2D A:HEM403 4.2 11.1 0.7 CA A:CYS345 4.2 6.5 1.0 C2D A:HEM403 4.2 8.9 0.3 C3A A:HEM403 4.2 11.0 0.3 C3D A:HEM403 4.2 9.1 0.3 C2C A:HEM403 4.2 11.2 0.7 C3C A:HEM403 4.2 7.7 0.3 C3A A:HEM403 4.2 8.9 0.7 C2A A:HEM403 4.2 9.1 0.7 C3B A:HEM403 4.2 8.7 0.7 C2B A:HEM403 4.2 7.6 0.7 C2C A:HEM403 4.2 8.7 0.3 C3B A:HEM403 4.3 11.1 0.3 C2B A:HEM403 4.3 10.2 0.3 OG A:SER237 4.5 10.0 1.0 C24 A:KEB402 4.6 14.9 0.6 CB A:SER237 4.7 9.5 1.0 CD A:PRO346 4.8 10.8 1.0 C A:CYS345 4.9 11.1 1.0 N A:GLY347 5.0 9.9 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