5NX6
Crystal structure of 1,8-cineole synthase from Streptomyces clavuligerus in complex with 2-fluoroneryl diphosphate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0010333 | molecular_function | terpene synthase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016838 | molecular_function | carbon-oxygen lyase activity, acting on phosphates |
| A | 0033383 | biological_process | geranyl diphosphate metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0102313 | molecular_function | 1,8-cineole synthase activity |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0010333 | molecular_function | terpene synthase activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016838 | molecular_function | carbon-oxygen lyase activity, acting on phosphates |
| B | 0033383 | biological_process | geranyl diphosphate metabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0102313 | molecular_function | 1,8-cineole synthase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | binding site for residue LA6 A 401 |
| Chain | Residue |
| A | PHE77 |
| A | SER224 |
| A | LYS227 |
| A | GLU228 |
| A | ASN305 |
| A | CYS309 |
| A | ARG314 |
| A | TYR315 |
| A | MG402 |
| A | MG403 |
| A | HOH502 |
| A | PHE78 |
| A | HOH505 |
| A | HOH524 |
| A | HOH530 |
| A | HOH569 |
| A | HOH693 |
| A | ASP81 |
| A | ARG174 |
| A | PHE179 |
| A | MET180 |
| A | ILE216 |
| A | ASN217 |
| A | ASN220 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 402 |
| Chain | Residue |
| A | ASN220 |
| A | SER224 |
| A | GLU228 |
| A | LA6401 |
| A | HOH524 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 403 |
| Chain | Residue |
| A | ASP81 |
| A | LA6401 |
| A | HOH501 |
| A | HOH502 |
| A | HOH505 |
| A | HOH508 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue 9D2 A 404 |
| Chain | Residue |
| A | GLU6 |
| A | LEU253 |
| A | ARG257 |
| B | ASP40 |
| B | GLU43 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue NDS A 405 |
| Chain | Residue |
| A | PHE19 |
| A | ARG22 |
| A | ARG26 |
| A | GLN63 |
| A | GLY64 |
| A | HOH550 |
| A | HOH694 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 406 |
| Chain | Residue |
| A | GLY282 |
| A | ILE283 |
| A | ARG288 |
| A | HOH561 |
| A | HOH702 |
| A | HOH758 |
| site_id | AC7 |
| Number of Residues | 24 |
| Details | binding site for residue LA6 B 401 |
| Chain | Residue |
| B | PHE77 |
| B | PHE78 |
| B | ASP81 |
| B | ARG174 |
| B | PHE179 |
| B | MET180 |
| B | ILE216 |
| B | ASN217 |
| B | ASN220 |
| B | SER224 |
| B | LYS227 |
| B | GLU228 |
| B | ASN305 |
| B | CYS309 |
| B | ARG314 |
| B | TYR315 |
| B | MG402 |
| B | MG403 |
| B | HOH502 |
| B | HOH509 |
| B | HOH512 |
| B | HOH520 |
| B | HOH565 |
| B | HOH695 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 402 |
| Chain | Residue |
| B | ASN220 |
| B | SER224 |
| B | GLU228 |
| B | LA6401 |
| B | HOH509 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 403 |
| Chain | Residue |
| B | ASP81 |
| B | LA6401 |
| B | HOH501 |
| B | HOH502 |
| B | HOH512 |
| B | HOH515 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue 9D2 B 404 |
| Chain | Residue |
| A | GLU43 |
| B | GLU6 |
| B | LEU253 |
| B | ARG257 |
| B | HOH530 |
| site_id | AD2 |
| Number of Residues | 8 |
| Details | binding site for residue NDS B 405 |
| Chain | Residue |
| B | HOH644 |
| B | HOH693 |
| A | PRO18 |
| B | PHE19 |
| B | ARG22 |
| B | ARG26 |
| B | GLN63 |
| B | GLY64 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 406 |
| Chain | Residue |
| B | GLY282 |
| B | ILE283 |
| B | ARG288 |
| B | HOH513 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Motif: {"description":"DDXXD motif","evidences":[{"source":"PubMed","id":"28966840","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | Motif: {"description":"NXXXSXXXE motif","evidences":[{"source":"PubMed","id":"28966840","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"28966840","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5NX6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5NX7","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"28966840","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5NX7","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
