1DMH
STRUCTURE OF CATECHOL 1,2-DIOXYGENASE FROM ACINETOBACTER SP. ADP1 WITH BOUND 4-METHYLCATECHOL
Summary for 1DMH
Entry DOI | 10.2210/pdb1dmh/pdb |
Related | 1DLM 1DLQ 1DLT |
Descriptor | CATECHOL 1,2-DIOXYGENASE, FE (III) ION, 4-METHYLCATECHOL, ... (5 entities in total) |
Functional Keywords | dioxygenase, aromatic hydrocarbon degradation, alpha/beta fold, metalloenzyme, substrate, oxidoreductase |
Biological source | Acinetobacter sp. |
Total number of polymer chains | 2 |
Total formula weight | 70401.98 |
Authors | Vetting, M.W.,Ohlendorf, D.H. (deposition date: 1999-12-14, release date: 2000-05-23, Last modification date: 2024-02-07) |
Primary citation | Vetting, M.W.,Ohlendorf, D.H. The 1.8 A crystal structure of catechol 1,2-dioxygenase reveals a novel hydrophobic helical zipper as a subunit linker. Structure Fold.Des., 8:429-440, 2000 Cited by PubMed: 10801478DOI: 10.1016/S0969-2126(00)00122-2 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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