9Q3I
Cryo-EM Structure of the Class II Cyclase Domain in the Bifunctional Copalyl Diphosphate Synthase from Penicillium verruculosum
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004311 | molecular_function | geranylgeranyl diphosphate synthase activity |
| A | 0004659 | molecular_function | prenyltransferase activity |
| A | 0008299 | biological_process | isoprenoid biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0043386 | biological_process | mycotoxin biosynthetic process |
| A | 0046165 | biological_process | alcohol biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050559 | molecular_function | copalyl diphosphate synthase activity |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Motif: {"description":"DXDD","evidences":[{"source":"PubMed","id":"28869716","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"31978464","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Motif: {"description":"NSE/DTE","evidences":[{"source":"PubMed","id":"28869716","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"31978464","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q40577","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"A2PZA5","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
