1XFG
Glutaminase domain of glucosamine 6-phosphate synthase complexed with l-glu hydroxamate
Replaces: 1GMSFunctional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA A 5301 |
| Chain | Residue |
| A | GLY154 |
| A | SER174 |
| A | HOH5356 |
| A | HOH5397 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA B 9301 |
| Chain | Residue |
| B | GLY154 |
| B | TYR156 |
| B | SER174 |
| B | HOH9359 |
| B | HOH9385 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACT A 5302 |
| Chain | Residue |
| A | HOH5333 |
| A | HOH5334 |
| A | HOH5432 |
| A | HOH5436 |
| B | ARG173 |
| B | PRO177 |
| B | SER191 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE HGA A 5300 |
| Chain | Residue |
| A | CYS1 |
| A | ARG73 |
| A | TRP74 |
| A | THR76 |
| A | HIS77 |
| A | HIS86 |
| A | HIS97 |
| A | ASN98 |
| A | GLY99 |
| A | ASP123 |
| A | THR124 |
| A | HOH5359 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE HGA B 9300 |
| Chain | Residue |
| B | CYS1 |
| B | ARG73 |
| B | TRP74 |
| B | THR76 |
| B | HIS77 |
| B | HIS86 |
| B | HIS97 |
| B | ASN98 |
| B | GLY99 |
| B | ASP123 |
| B | THR124 |
| B | HOH9326 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 432 |
| Details | Domain: {"description":"Glutamine amidotransferase type-2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile; for GATase activity","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ecf |
| Chain | Residue | Details |
| A | ASN98 | |
| A | GLY99 | |
| A | CYS1 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ecf |
| Chain | Residue | Details |
| B | ASN98 | |
| B | GLY99 | |
| B | CYS1 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 82 |
| Chain | Residue | Details |
| A | CYS1 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | ARG26 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| A | TRP74 | electrostatic stabiliser, hydrogen bond donor |
| A | ASN98 | electrostatic stabiliser, hydrogen bond donor |
| A | GLY99 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 82 |
| Chain | Residue | Details |
| B | CYS1 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| B | ARG26 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| B | TRP74 | electrostatic stabiliser, hydrogen bond donor |
| B | ASN98 | electrostatic stabiliser, hydrogen bond donor |
| B | GLY99 | electrostatic stabiliser, hydrogen bond donor |
