1FWK
CRYSTAL STRUCTURE OF HOMOSERINE KINASE COMPLEXED WITH ADP
Summary for 1FWK
Entry DOI | 10.2210/pdb1fwk/pdb |
Related | 1FWL |
Descriptor | HOMOSERINE KINASE, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total) |
Functional Keywords | kinase, transferase |
Biological source | Methanocaldococcus jannaschii |
Cellular location | Cytoplasm : Q58504 |
Total number of polymer chains | 4 |
Total formula weight | 130930.59 |
Authors | Zhou, T.,Daugherty, M.,Grishin, N.V.,Osterman, A.L.,Zhang, H. (deposition date: 2000-09-22, release date: 2000-12-20, Last modification date: 2024-02-07) |
Primary citation | Zhou, T.,Daugherty, M.,Grishin, N.V.,Osterman, A.L.,Zhang, H. Structure and mechanism of homoserine kinase: prototype for the GHMP kinase superfamily. Structure Fold.Des., 8:1247-1257, 2000 Cited by PubMed Abstract: Homoserine kinase (HSK) catalyzes an important step in the threonine biosynthesis pathway. It belongs to a large yet unique class of small metabolite kinases, the GHMP kinase superfamily. Members in the GHMP superfamily participate in several essential metabolic pathways, such as amino acid biosynthesis, galactose metabolism, and the mevalonate pathway. PubMed: 11188689DOI: 10.1016/S0969-2126(00)00533-5 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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