12AS
ASPARAGINE SYNTHETASE MUTANT C51A, C315A COMPLEXED WITH L-ASPARAGINE AND AMP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004071 | molecular_function | aspartate-ammonia ligase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006529 | biological_process | asparagine biosynthetic process |
| A | 0006974 | biological_process | DNA damage response |
| A | 0016874 | molecular_function | ligase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0070981 | biological_process | L-asparagine biosynthetic process |
| B | 0004071 | molecular_function | aspartate-ammonia ligase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006529 | biological_process | asparagine biosynthetic process |
| B | 0006974 | biological_process | DNA damage response |
| B | 0016874 | molecular_function | ligase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| 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 ASN A 331 |
| Chain | Residue |
| A | SER251 |
| A | ARG255 |
| A | GLY293 |
| A | GLY294 |
| A | AMP332 |
| A | HOH371 |
| A | ASP46 |
| A | SER72 |
| A | ALA74 |
| A | LYS77 |
| A | GLN116 |
| A | ASP118 |
| A | TYR218 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ASN B 331 |
| Chain | Residue |
| B | ASP46 |
| B | SER72 |
| B | ALA74 |
| B | LYS77 |
| B | GLN116 |
| B | ASP118 |
| B | TYR218 |
| B | ASP219 |
| B | SER251 |
| B | ARG255 |
| B | GLY292 |
| B | GLY293 |
| B | AMP332 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE AMP A 332 |
| Chain | Residue |
| A | ARG100 |
| A | GLU103 |
| A | LEU109 |
| A | HIS110 |
| A | SER111 |
| A | VAL114 |
| A | GLN116 |
| A | GLU248 |
| A | LEU249 |
| A | SER250 |
| A | SER251 |
| A | GLY294 |
| A | GLY296 |
| A | ARG299 |
| A | ILE310 |
| A | ASN331 |
| A | HOH386 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE AMP B 332 |
| Chain | Residue |
| B | ARG100 |
| B | GLU103 |
| B | LEU109 |
| B | HIS110 |
| B | SER111 |
| B | VAL114 |
| B | GLN116 |
| B | GLU248 |
| B | LEU249 |
| B | SER250 |
| B | SER251 |
| B | GLY296 |
| B | ARG299 |
| B | ASN331 |
| B | HOH385 |
| site_id | NU1 |
| Number of Residues | 1 |
| Details | AMP BINDING (CATALYTIC) SITE (CHAIN A). |
| Chain | Residue |
| A | AMP332 |
| site_id | NU2 |
| Number of Residues | 1 |
| Details | AMP BINDING (CATALYTIC) SITE (CHAIN B). |
| Chain | Residue |
| B | AMP332 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 9437423 |
| Chain | Residue | Details |
| A | ASP46 | |
| A | GLN116 | |
| A | ARG100 |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 75 |
| Chain | Residue | Details |
| A | ASP46 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | ARG100 | electrostatic stabiliser, hydrogen bond donor |
| A | GLN116 | electrostatic stabiliser, hydrogen bond donor |
| A | ASP235 | metal ligand |
| A | GLU248 | metal ligand |
| A | SER251 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 75 |
| Chain | Residue | Details |
| B | ASP46 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | ARG100 | electrostatic stabiliser, hydrogen bond donor |
| B | GLN116 | electrostatic stabiliser, hydrogen bond donor |
| B | ASP235 | metal ligand |
| B | GLU248 | metal ligand |
| B | SER251 | electrostatic stabiliser |
