1DIQ
CRYSTAL STRUCTURE OF P-CRESOL METHYLHYDROXYLASE WITH SUBSTRATE BOUND
Summary for 1DIQ
Entry DOI | 10.2210/pdb1diq/pdb |
Related | 1DII |
Descriptor | P-CRESOL METHYLHYDROXYLASE, CHLORIDE ION, FLAVIN-ADENINE DINUCLEOTIDE, ... (7 entities in total) |
Functional Keywords | flavocytochrome, electron-transfer, fad, heme, p-cresol, oxidoreductase |
Biological source | Pseudomonas putida More |
Total number of polymer chains | 4 |
Total formula weight | 136330.50 |
Authors | Cunane, L.M.,Chen, Z.W.,Shamala, N.,Mathews, F.S.,Cronin, C.S.,McIntire, W.S. (deposition date: 1999-11-29, release date: 1999-12-08, Last modification date: 2021-03-03) |
Primary citation | Cunane, L.M.,Chen, Z.W.,Shamala, N.,Mathews, F.S.,Cronin, C.N.,McIntire, W.S. Structures of the flavocytochrome p-cresol methylhydroxylase and its enzyme-substrate complex: gated substrate entry and proton relays support the proposed catalytic mechanism. J.Mol.Biol., 295:357-374, 2000 Cited by PubMed: 10623531DOI: 10.1006/jmbi.1999.3290 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.75 Å) |
Structure validation
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