4LIX
Crystal structure of ent-copalyl diphosphate synthase from Arabidopsis thaliana in complex with (S)-15-aza-14,15-dihydrogeranylgeranyl thiolodiphosphate at 1.55 A resolution
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0006721 | biological_process | terpenoid metabolic process |
A | 0008299 | biological_process | isoprenoid biosynthetic process |
A | 0009507 | cellular_component | chloroplast |
A | 0009536 | cellular_component | plastid |
A | 0009686 | biological_process | gibberellin biosynthetic process |
A | 0009740 | biological_process | gibberellic acid mediated signaling pathway |
A | 0009905 | molecular_function | ent-copalyl diphosphate synthase activity |
A | 0010333 | molecular_function | terpene synthase activity |
A | 0016102 | biological_process | diterpenoid biosynthetic process |
A | 0016114 | biological_process | terpenoid biosynthetic process |
A | 0016829 | molecular_function | lyase activity |
A | 0016853 | molecular_function | isomerase activity |
A | 0033993 | biological_process | response to lipid |
A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE AG8 A 901 |
Chain | Residue |
A | ILE208 |
A | LYS463 |
A | TRP464 |
A | HOH1498 |
A | HOH1531 |
A | HOH1544 |
A | GLY209 |
A | LYS245 |
A | THR260 |
A | HIS263 |
A | PHE329 |
A | TRP333 |
A | PHE412 |
A | ASN417 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PO4 A 902 |
Chain | Residue |
A | HIS182 |
A | LYS186 |
A | SER579 |
A | HIS580 |
A | SER663 |
A | HIS664 |
A | HOH1279 |
A | HOH1562 |
A | HOH1666 |
site_id | AC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL A 903 |
Chain | Residue |
A | ARG192 |
A | PRO229 |
A | HIS789 |
A | GLN791 |
A | THR792 |
A | HOH1030 |
A | HOH1082 |
A | HOH1200 |
A | HOH1419 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21602811, ECO:0007744|PDB:3PYA |
Chain | Residue | Details |
A | LYS245 | |
A | LYS463 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:C7BKP9 |
Chain | Residue | Details |
A | ASP377 | |
A | ASP379 |