6RQD
CYP121 in complex with 3-chloro dicyclotyrosine
Summary for 6RQD
| Entry DOI | 10.2210/pdb6rqd/pdb |
| Descriptor | Mycocyclosin synthase, SULFATE ION, (3~{S},6~{S})-3-[(3-chloranyl-4-oxidanyl-phenyl)methyl]-6-[(4-hydroxyphenyl)methyl]piperazine-2,5-dione, ... (5 entities in total) |
| Functional Keywords | cyp121, p450, dicyclotyrosine derivatives, heme, oxidoreductase |
| Biological source | Mycobacterium tuberculosis |
| Total number of polymer chains | 1 |
| Total formula weight | 44571.33 |
| Authors | Poddar, H.,Levy, C. (deposition date: 2019-05-15, release date: 2020-04-22, Last modification date: 2024-01-24) |
| Primary citation | Rajput, S.,McLean, K.J.,Poddar, H.,Selvam, I.R.,Nagalingam, G.,Triccas, J.A.,Levy, C.W.,Munro, A.W.,Hutton, C.A. Structure-Activity Relationships of cyclo (l-Tyrosyl-l-tyrosine) Derivatives Binding to Mycobacterium tuberculosis CYP121: Iodinated Analogues Promote Shift to High-Spin Adduct. J.Med.Chem., 62:9792-9805, 2019 Cited by PubMed Abstract: A series of analogues of (l-tyrosyl-l-tyrosine), the substrate of the enzyme CYP121, have been synthesized and analyzed by UV-vis and electron paramagnetic resonance spectroscopy and by X-ray crystallography. The introduction of iodine substituents onto (l-tyrosyl-l-tyrosine) results in sub-μM binding affinity for the CYP121 enzyme and a complete shift to the high-spin state of the heme Fe. The introduction of halogens that are able to interact with heme groups is thus a feasible approach to the development of next-generation, tight binding inhibitors of the CYP121 enzyme, in the search for novel antitubercular compounds. PubMed: 31618032DOI: 10.1021/acs.jmedchem.9b01199 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.499 Å) |
Structure validation
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