1MKI
Crystal Structure of Bacillus Subtilis Probable Glutaminase, APC1040
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004359 | molecular_function | glutaminase activity |
| A | 0006537 | biological_process | glutamate biosynthetic process |
| A | 0006541 | biological_process | glutamine metabolic process |
| A | 0006543 | biological_process | glutamine catabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| B | 0004359 | molecular_function | glutaminase activity |
| B | 0006537 | biological_process | glutamate biosynthetic process |
| B | 0006541 | biological_process | glutamine metabolic process |
| B | 0006543 | biological_process | glutamine catabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 1302 |
| Chain | Residue |
| A | PHE262 |
| A | LYS316 |
| A | EDO1303 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 1303 |
| Chain | Residue |
| A | TYR259 |
| A | GLY312 |
| A | EDO1302 |
| A | HOH1386 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 1305 |
| Chain | Residue |
| A | ASN188 |
| A | PHE189 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO B 1304 |
| Chain | Residue |
| B | GLY312 |
| B | HOH1445 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE FMT A 1301 |
| Chain | Residue |
| A | ASP98 |
| A | PHE121 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | SEP74 | |
| B | GLU170 | |
| B | ASN177 | |
| B | TYR201 | |
| B | TYR253 | |
| B | VAL271 | |
| A | ASN126 | |
| A | GLU170 | |
| A | ASN177 | |
| A | TYR201 | |
| A | TYR253 | |
| A | VAL271 | |
| B | SEP74 | |
| B | ASN126 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 301 |
| Chain | Residue | Details |
| A | SEP74 | activator, covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | LYS77 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | TYR201 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | TYR253 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | VAL271 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 301 |
| Chain | Residue | Details |
| B | SEP74 | activator, covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| B | LYS77 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | TYR201 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| B | TYR253 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| B | VAL271 | electrostatic stabiliser, hydrogen bond donor |
