Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0010223 | biological_process | secondary shoot formation |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| A | 1901601 | biological_process | strigolactone biosynthetic process |
| B | 0010223 | biological_process | secondary shoot formation |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| B | 1901601 | biological_process | strigolactone biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | binding site for residue MES A 301 |
| Chain | Residue |
| A | SER96 |
| A | HOH445 |
| A | HOH531 |
| A | PHE125 |
| A | PHE135 |
| A | PHE158 |
| A | VAL193 |
| A | PHE194 |
| A | SER219 |
| A | HIS246 |
| A | HOH433 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 302 |
| Chain | Residue |
| A | HOH408 |
| A | HOH413 |
| A | HOH588 |
| B | HOH408 |
| B | HOH415 |
| B | HOH613 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 303 |
| Chain | Residue |
| A | TYR131 |
| A | HIS132 |
| A | SER223 |
| A | VAL224 |
| A | TYR227 |
| A | HOH493 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | binding site for residue MES B 301 |
| Chain | Residue |
| B | SER96 |
| B | PHE125 |
| B | PHE135 |
| B | PHE158 |
| B | PHE194 |
| B | SER219 |
| B | HIS246 |
| B | HOH406 |
| B | HOH460 |
| B | HOH509 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 302 |
| Chain | Residue |
| B | HOH472 |
| B | HOH477 |
| B | HOH507 |
| B | HOH615 |
| B | HOH633 |
| B | HOH639 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 303 |
| Chain | Residue |
| A | HOH419 |
| A | HOH431 |
| A | HOH569 |
| B | ASP72 |
| B | HOH420 |
| B | HOH429 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 304 |
| Chain | Residue |
| B | ASN10 |
| B | HOH421 |
| B | HOH473 |
| B | HOH550 |
| B | HOH571 |
| B | HOH629 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue MG B 305 |
| Chain | Residue |
| B | HOH587 |
| B | HOH642 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue MG B 306 |
| Chain | Residue |
| B | HOH422 |
| B | HOH515 |
| B | HOH599 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue MG B 307 |
| Chain | Residue |
| B | HIS231 |
| B | HOH450 |
| B | HOH619 |
| B | HOH623 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 B 308 |
| Chain | Residue |
| B | PRO221 |
| B | ALA222 |
| B | SER223 |
| B | HOH477 |
| B | HOH507 |
| B | HOH516 |
| B | HOH521 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 309 |
| Chain | Residue |
| A | HOH417 |
| B | ARG108 |
| B | ARG109 |
| B | HOH537 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 B 310 |
| Chain | Residue |
| B | ARG36 |
| B | ALA252 |
| B | PRO253 |
| B | THR254 |
| B | HOH404 |
| B | HOH481 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 311 |
| Chain | Residue |
| B | GLU18 |
| B | TYR131 |
| B | HIS132 |
| B | SER223 |
| B | VAL224 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"22959345","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"UniProtKB","id":"Q10QA5","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"22959345","evidenceCode":"ECO:0000269"}]} |
