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

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 molecular weight34482.14
Evans III, R.L.,Wilmot, C.M. (deposition date: 2018-07-09, release date: 2019-05-22, Last modification date: 2020-01-01)
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
PubMed: 30811189 (PDB entries with the same primary citation)
DOI: 10.1021/jacs.8b13453
MImport into Mendeley
Experimental method

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers 0.2365 0.3% 0.8% 2.6%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
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