1CC4
PHE161 AND ARG166 VARIANTS OF P-HYDROXYBENZOATE HYDROXYLASE. IMPLICATIONS FOR NADPH RECOGNITION AND STRUCTURAL STABILITY.
Summary for 1CC4
Entry DOI | 10.2210/pdb1cc4/pdb |
Descriptor | PROTEIN (P-HYDROXYBENZOATE HYDROXYLASE), FLAVIN-ADENINE DINUCLEOTIDE, P-HYDROXYBENZOIC ACID, ... (4 entities in total) |
Functional Keywords | oxidoreductase, hydroxybenzoate |
Biological source | Pseudomonas fluorescens |
Total number of polymer chains | 1 |
Total formula weight | 45212.08 |
Authors | Eppink, M.H.M.,Bunthof, C.,Schreuder, H.A.,Van Berkel, W.J.H. (deposition date: 1999-03-04, release date: 1999-03-12, Last modification date: 2023-08-09) |
Primary citation | Eppink, M.H.,Bunthol, C.,Schreuder, H.A.,van Berkel, W.J. Phe161 and Arg166 variants of p-hydroxybenzoate hydroxylase. Implications for NADPH recognition and structural stability. Febs Lett., 443:251-255, 1999 Cited by PubMed: 10025942DOI: 10.1016/S0014-5793(98)01726-8 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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