3BRM
Crystal structure of the covalent complex between the Bacillus subtilis glutaminase YbgJ and 5-oxo-L-norleucine formed by reaction of the protein with 6-diazo-5-oxo-L-norleucine
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 | L-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 | L-glutamine catabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ONL A 401 |
| Chain | Residue |
| A | GLN73 |
| A | SER74 |
| A | LYS77 |
| A | ASN126 |
| A | GLU170 |
| A | ASN177 |
| A | TYR201 |
| A | TYR253 |
| A | GLY270 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ONL B 401 |
| Chain | Residue |
| B | TYR37 |
| B | GLN73 |
| B | SER74 |
| B | LYS77 |
| B | ASN126 |
| B | GLU170 |
| B | ASN177 |
| B | TYR201 |
| B | CYS205 |
| B | TYR253 |
| B | GLY270 |
| B | HOH536 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | SER74 | |
| B | GLU170 | |
| B | ASN177 | |
| B | TYR201 | |
| B | TYR253 | |
| B | VAL271 | |
| A | ASN126 | |
| A | GLU170 | |
| A | ASN177 | |
| A | TYR201 | |
| A | TYR253 | |
| A | VAL271 | |
| B | SER74 | |
| B | ASN126 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 301 |
| Chain | Residue | Details |
| A | MSE86 | activator, covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | GLY89 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | GLY225 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | PHE289 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | ASN307 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 301 |
| Chain | Residue | Details |
| B | MSE86 | activator, covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| B | GLY89 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | GLY225 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| B | PHE289 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| B | ASN307 | electrostatic stabiliser, hydrogen bond donor |
