6E13
Pseudomonas putida PqqB with a non-physiological zinc at the active site binds the substrate mimic, 5-cysteinyl-3,4-dihydroxyphenylalanine (5-Cys-DOPA), non-specifically but supports the proposed function of the enzyme in pyrroloquinoline quinone biosynthesis.
Summary for 6E13
Entry DOI | 10.2210/pdb6e13/pdb |
Descriptor | Coenzyme PQQ synthesis protein B, ZINC ION, CHLORIDE ION, ... (5 entities in total) |
Functional Keywords | iron-dependent, hydroxylase, metallo beta-lactamase, oxidoreductase |
Biological source | Pseudomonas putida (strain ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440) |
Total number of polymer chains | 1 |
Total formula weight | 34482.14 |
Authors | Evans III, R.L.,Wilmot, C.M. (deposition date: 2018-07-09, release date: 2019-05-22, Last modification date: 2024-03-13) |
Primary citation | Koehn, E.M.,Latham, J.A.,Armand, T.,Evans 3rd, R.L.,Tu, X.,Wilmot, C.M.,Iavarone, A.T.,Klinman, J.P. Discovery of Hydroxylase Activity for PqqB Provides a Missing Link in the Pyrroloquinoline Quinone Biosynthetic Pathway. J.Am.Chem.Soc., 141:4398-4405, 2019 Cited by PubMed: 30811189DOI: 10.1021/jacs.8b13453 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.349 Å) |
Structure validation
Download full validation report