3UJN
Formyl Glycinamide Ribonucleotide Amidotransferase from Salmonella Typhimurium : Role of the ATP complexation and glutaminase domain in catalytic coupling
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0004642 | molecular_function | phosphoribosylformylglycinamidine synthase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0006164 | biological_process | purine nucleotide biosynthetic process |
A | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
A | 0016874 | molecular_function | ligase activity |
A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 A 2002 |
Chain | Residue |
A | THR295 |
A | ASN297 |
A | HIS298 |
A | LYS409 |
A | SER778 |
A | HOH1437 |
A | HOH1499 |
A | HOH1511 |
site_id | AC2 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE ADP A 2005 |
Chain | Residue |
A | THR386 |
A | GLY387 |
A | TYR388 |
A | LYS649 |
A | LEU652 |
A | VAL653 |
A | GLN668 |
A | PRO676 |
A | ALA678 |
A | ASP679 |
A | GLU718 |
A | ASN722 |
A | SER886 |
A | HOH1533 |
A | MG2006 |
A | MG2007 |
A | MG2008 |
A | VAL333 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE MG A 2006 |
Chain | Residue |
A | GLU718 |
A | ADP2005 |
site_id | AC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE MG A 2007 |
Chain | Residue |
A | SER886 |
A | ADP2005 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 2008 |
Chain | Residue |
A | ASP679 |
A | ASN722 |
A | ASP884 |
A | SER886 |
A | ADP2005 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 2009 |
Chain | Residue |
A | SER12 |
A | ALA13 |
A | PHE14 |
A | ASN998 |
A | HIS1161 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 22 |
Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | Active site: {"description":"Nucleophile","evidences":[{"source":"HAMAP-Rule","id":"MF_00419","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00419","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 11 |
Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00419","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | Binding site: {} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00419","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15301531","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22683785","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24223728","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |