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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 DOI10.2210/pdb6e13/pdb
DescriptorCoenzyme PQQ synthesis protein B, ZINC ION, CHLORIDE ION, ... (5 entities in total)
Functional Keywordsiron-dependent, hydroxylase, metallo beta-lactamase, oxidoreductase
Biological sourcePseudomonas putida (strain ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440)
Total number of polymer chains1
Total formula weight34482.14
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 citationKoehn, 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: 30811189
DOI: 10.1021/jacs.8b13453
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.349 Å)
Structure validation

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