3UGS
Crystal structure of a probable undecaprenyl diphosphate synthase (uppS) from Campylobacter jejuni
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004659 | molecular_function | prenyltransferase activity |
| A | 0016094 | biological_process | polyprenol biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
| A | 0045547 | molecular_function | ditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyl diphosphate specific] activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004659 | molecular_function | prenyltransferase activity |
| B | 0016094 | biological_process | polyprenol biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
| B | 0045547 | molecular_function | ditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyl diphosphate specific] activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE FFT B 401 |
| Chain | Residue |
| A | THR220 |
| B | ARG178 |
| B | SER180 |
| B | HOH237 |
| B | VAL10 |
| B | MET11 |
| B | ASP12 |
| B | GLY13 |
| B | PHE55 |
| B | ALA56 |
| B | ASN61 |
| B | ARG172 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE FFT A 401 |
| Chain | Residue |
| A | MET11 |
| A | ASP12 |
| A | GLY13 |
| A | PHE55 |
| A | ALA56 |
| A | ASN61 |
| A | LEU76 |
| A | ARG172 |
| A | ARG178 |
| A | SER180 |
| A | HOH248 |
| B | THR220 |
Functional Information from PROSITE/UniProt
| site_id | PS01066 |
| Number of Residues | 18 |
| Details | UPP_SYNTHASE Undecaprenyl pyrophosphate synthase family signature. DLMLRVGNakRlSnFLLW |
| Chain | Residue | Details |
| B | ASP168-TRP185 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2011","submissionDatabase":"PDB data bank","title":"Crystal structure of a probable undecaprenyl diphosph synthase (upps) from campylobacter jejuni.","authors":["Nocek B.","Gu M.","Grimshaw S.","Anderson W.F.","Joachimiak A."]}}]} |
| Chain | Residue | Details |
