3G59
Crystal Structure of Candida glabrata FMN Adenylyltransferase in complex with ATP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003919 | molecular_function | FMN adenylyltransferase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005575 | cellular_component | cellular_component |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005829 | cellular_component | cytosol |
| A | 0006747 | biological_process | FAD biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE ATP A 305 |
| Chain | Residue |
| A | SER60 |
| A | ILE108 |
| A | ILE162 |
| A | GLY163 |
| A | ILE164 |
| A | ARG165 |
| A | ASP168 |
| A | TYR216 |
| A | SER222 |
| A | LEU223 |
| A | GLU296 |
| A | TYR61 |
| A | ACT306 |
| A | HOH322 |
| A | HOH445 |
| A | ASN62 |
| A | GLY64 |
| A | LYS65 |
| A | ASP66 |
| A | CYS67 |
| A | VAL106 |
| A | PHE107 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT A 306 |
| Chain | Residue |
| A | SER60 |
| A | MET143 |
| A | PHE147 |
| A | ATP305 |
| A | HOH478 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE POP A 307 |
| Chain | Residue |
| A | ASN119 |
| A | ALA270 |
| A | ASP271 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19375431","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3G6K","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P38913","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19375431","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3G59","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19375431","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3G5A","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3G6K","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19375431","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3G5A","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"3G5A","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"3G59","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"3G6K","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
