2C5H
X-ray crystal structure of 5'-fluorodeoxyadenosine synthase from Streptomyces cattleya complexed with 2'deoxy-adenosine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016740 | molecular_function | transferase activity |
| A | 0033846 | molecular_function | adenosyl-fluoride synthase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0033846 | molecular_function | adenosyl-fluoride synthase activity |
| C | 0016740 | molecular_function | transferase activity |
| C | 0033846 | molecular_function | adenosyl-fluoride synthase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MET A1301 |
| Chain | Residue |
| A | ASP210 |
| A | TRP217 |
| A | SER269 |
| A | ARG270 |
| A | HOH2027 |
| C | ASP21 |
| C | SER23 |
| C | THR155 |
| C | PHE156 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MET B1299 |
| Chain | Residue |
| A | ASP21 |
| A | SER23 |
| A | THR155 |
| A | 3D1500 |
| B | ASP210 |
| B | PHE213 |
| B | TRP217 |
| B | SER269 |
| B | ARG270 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 3D1 A 500 |
| Chain | Residue |
| A | ASP16 |
| A | TRP50 |
| A | TYR77 |
| A | PRO78 |
| A | THR80 |
| A | THR155 |
| A | PHE156 |
| A | TYR157 |
| A | SER158 |
| B | PHE213 |
| B | ASN215 |
| B | PHE254 |
| B | ARG277 |
| B | ALA279 |
| B | MET1299 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 3D1 B 500 |
| Chain | Residue |
| A | PHE213 |
| A | ASN215 |
| A | PHE254 |
| A | ARG277 |
| A | ALA279 |
| A | ALA280 |
| C | ASP16 |
| C | TRP50 |
| C | THR76 |
| C | TYR77 |
| C | PRO78 |
| C | THR155 |
| C | PHE156 |
| C | TYR157 |
| C | SER158 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE 3D1 C 500 |
| Chain | Residue |
| B | ASP16 |
| B | TRP50 |
| B | TYR77 |
| B | PRO78 |
| B | THR155 |
| B | PHE156 |
| B | TYR157 |
| B | SER158 |
| C | PHE213 |
| C | ASN215 |
| C | PHE254 |
| C | ARG277 |
| C | ALA279 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 30 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"14765200","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16370017","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16604208","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17985882","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"OCT-2005","submissionDatabase":"PDB data bank","title":"Substrates and inhibitors of the fluorinase from Streptomyces cattleya.","authors":["Mcewan A.R.","Deng H.","Mcglinchey R.P.","Robinson D.R.","O'Hagan D.","Naismith J.H."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2014","submissionDatabase":"PDB data bank","title":"Structure of a bacterial fluorinating enzyme with.","authors":["Thomson S.","Mcmahon S.A.","Naismith J.H.","O'Hagan D."]}}]} |
| Chain | Residue | Details |
