6GQ3
Human asparagine synthetase (ASNS) in complex with 6-diazo-5-oxo-L-norleucine (DON) at 1.85 A resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004066 | molecular_function | asparagine synthase (glutamine-hydrolyzing) activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0042149 | biological_process | cellular response to glucose starvation |
| A | 0043066 | biological_process | negative regulation of apoptotic process |
| A | 0045931 | biological_process | positive regulation of mitotic cell cycle |
| A | 0070981 | biological_process | L-asparagine biosynthetic process |
| B | 0004066 | molecular_function | asparagine synthase (glutamine-hydrolyzing) activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0042149 | biological_process | cellular response to glucose starvation |
| B | 0043066 | biological_process | negative regulation of apoptotic process |
| B | 0045931 | biological_process | positive regulation of mitotic cell cycle |
| B | 0070981 | biological_process | L-asparagine biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | binding site for residue ONL A 601 |
| Chain | Residue |
| A | CYS1 |
| A | VAL95 |
| A | ASP96 |
| A | HOH707 |
| A | HOH720 |
| A | ARG48 |
| A | LEU49 |
| A | VAL51 |
| A | VAL52 |
| A | TYR73 |
| A | ASN74 |
| A | GLY75 |
| A | GLU76 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 602 |
| Chain | Residue |
| A | ARG62 |
| A | LYS64 |
| A | GLN92 |
| A | HOH914 |
| B | GLN92 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 603 |
| Chain | Residue |
| A | CYS114 |
| A | MET115 |
| A | LEU116 |
| A | CYS206 |
| A | HIS422 |
| A | HOH702 |
| A | HOH902 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 604 |
| Chain | Residue |
| A | PRO505 |
| A | PHE506 |
| A | ARG518 |
| A | GLU522 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residue EPE A 605 |
| Chain | Residue |
| A | ASP334 |
| A | THR336 |
| A | TYR373 |
| A | ILE374 |
| A | TYR375 |
| A | PHE399 |
| A | HOH722 |
| A | HOH898 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue CL A 606 |
| Chain | Residue |
| A | TYR78 |
| A | ARG245 |
| A | ARG416 |
| A | VAL417 |
| A | HOH859 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 602 |
| Chain | Residue |
| A | GLN92 |
| B | ARG62 |
| B | LYS64 |
| B | GLN92 |
| B | HOH857 |
| B | HOH905 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | binding site for residue EPE B 603 |
| Chain | Residue |
| B | ASP334 |
| B | THR336 |
| B | TYR373 |
| B | ILE374 |
| B | TYR375 |
| B | PHE399 |
| B | HOH749 |
| B | HOH873 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue CL B 604 |
| Chain | Residue |
| B | TYR78 |
| B | ARG245 |
| B | ARG416 |
| B | VAL417 |
| B | HOH875 |
| site_id | AD1 |
| Number of Residues | 15 |
| Details | binding site for Di-peptide ONL B 601 and CYS B 1 |
| Chain | Residue |
| B | GLY2 |
| B | ARG26 |
| B | PHE46 |
| B | HIS47 |
| B | ARG48 |
| B | LEU49 |
| B | VAL51 |
| B | VAL52 |
| B | TYR73 |
| B | ASN74 |
| B | GLY75 |
| B | GLU76 |
| B | ASP96 |
| B | HOH712 |
| B | HOH715 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 378 |
| Details | Domain: {"description":"Glutamine amidotransferase type-2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00609","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"For GATase activity","evidences":[{"source":"PubMed","id":"2564390","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2573597","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Site: {"description":"Important for beta-aspartyl-AMP intermediate formation","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
