5C05
Crystal Structure of Gamma-terpinene Synthase from Thymus vulgaris
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0009751 | biological_process | response to salicylic acid |
| A | 0009753 | biological_process | response to jasmonic acid |
| A | 0010225 | biological_process | response to UV-C |
| 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 | 0016838 | molecular_function | carbon-oxygen lyase activity, acting on phosphates |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0102903 | molecular_function | gamma-terpinene synthase activity |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0009751 | biological_process | response to salicylic acid |
| B | 0009753 | biological_process | response to jasmonic acid |
| B | 0010225 | biological_process | response to UV-C |
| B | 0010333 | molecular_function | terpene synthase activity |
| B | 0016102 | biological_process | diterpenoid biosynthetic process |
| B | 0016114 | biological_process | terpenoid biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016838 | molecular_function | carbon-oxygen lyase activity, acting on phosphates |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0102903 | molecular_function | gamma-terpinene synthase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 601 |
| Chain | Residue |
| A | ASN117 |
| A | LEU247 |
| A | ARG250 |
| A | PHE259 |
| A | HOH913 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 602 |
| Chain | Residue |
| A | THR462 |
| A | HOH803 |
| A | TYR333 |
| A | ASP400 |
| A | ASP404 |
| A | GLN405 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 603 |
| Chain | Residue |
| A | ARG161 |
| A | LEU203 |
| A | ARG205 |
| A | ASN541 |
| A | MET544 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 604 |
| Chain | Residue |
| A | ARG312 |
| A | ARG314 |
| A | ILE315 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 601 |
| Chain | Residue |
| B | TYR333 |
| B | ASP400 |
| B | ASP404 |
| B | GLN405 |
| B | THR462 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 602 |
| Chain | Residue |
| B | TRP299 |
| B | ARG312 |
| B | ARG314 |
| B | ILE315 |
| B | CYS318 |
| B | HOH750 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 603 |
| Chain | Residue |
| B | ARG116 |
| B | ASN117 |
| B | LEU247 |
| B | ARG250 |
| B | PHE259 |
| B | HOH721 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 604 |
| Chain | Residue |
| B | GLU212 |
| B | TYR531 |
| B | ARG534 |
| B | GLN538 |
| B | HOH851 |
| B | HOH941 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 86 |
| Details | Region: {"description":"Homodimerization","evidences":[{"source":"PubMed","id":"26750479","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Motif: {"description":"DDXXD motif","evidences":[{"source":"UniProtKB","id":"Q9X839","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"A0A1C9J6A7","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Site: {"description":"Required for gamma-terpinene synthase activity","evidences":[{"source":"PubMed","id":"26750479","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
