7BUS
Chalcone synthase from Glycine max (L.) Merr (soybean)
Summary for 7BUS
| Entry DOI | 10.2210/pdb7bus/pdb |
| Descriptor | Chalcone synthase (2 entities in total) |
| Functional Keywords | isoflavonoid, flavonoid, soybean, plant protein, transferase |
| Biological source | Glycine max (Soybean) |
| Total number of polymer chains | 2 |
| Total formula weight | 89296.95 |
| Authors | Imaizumi, R.,Mameda, R.,Takeshita, K.,Waki, T.,Kubo, H.,Sakai, N.,Nakata, S.,Takahashi, S.,Kataoka, K.,Yamamoto, M.,Yamashita, S.,Nakayama, T. (deposition date: 2020-04-08, release date: 2020-08-19, Last modification date: 2023-11-29) |
| Primary citation | Imaizumi, R.,Mameda, R.,Takeshita, K.,Kubo, H.,Sakai, N.,Nakata, S.,Takahashi, S.,Kataoka, K.,Yamamoto, M.,Nakayama, T.,Yamashita, S.,Waki, T. Crystal structure of chalcone synthase, a key enzyme for isoflavonoid biosynthesis in soybean. Proteins, 2020 Cited by PubMed Abstract: Isoflavonoid is one of the groups of flavonoids that play pivotal roles in the survival of land plants. Chalcone synthase (CHS), the first enzyme of the isoflavonoid biosynthetic pathway, catalyzes the formation of a common isoflavonoid precursor. We have previously reported that an isozyme of soybean CHS (termed GmCHS1) is a key component of the isoflavonoid metabolon, a protein complex to enhance efficiency of isoflavonoid production. Here, we determined the crystal structure of GmCHS1 as a first step of understanding the metabolon structure, as well as to better understand the catalytic mechanism of GmCHS1. PubMed: 32725893DOI: 10.1002/prot.25988 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.52 Å) |
Structure validation
Download full validation report
