3UO9
Crystal Structure of Human GAC in Complex with Glutamate and BPTES
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004359 | molecular_function | glutaminase activity |
| A | 0006541 | biological_process | glutamine metabolic process |
| B | 0004359 | molecular_function | glutaminase activity |
| B | 0006541 | biological_process | glutamine metabolic process |
| C | 0004359 | molecular_function | glutaminase activity |
| C | 0006541 | biological_process | glutamine metabolic process |
| D | 0004359 | molecular_function | glutaminase activity |
| D | 0006541 | biological_process | glutamine metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details |
| Chain | Residue |
| A | LEU434 |
| C | ASN532 |
| C | HOH720 |
| A | ALA435 |
| A | GLY437 |
| A | PRO450 |
| A | VAL453 |
| A | ARG454 |
| A | LEU457 |
| A | HOH673 |
| C | TYR530 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details |
| Chain | Residue |
| A | GLU383 |
| A | ASP386 |
| A | PHE389 |
| B | TYR393 |
| B | LYS396 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details |
| Chain | Residue |
| A | LYS320 |
| A | LEU321 |
| A | PHE322 |
| A | LEU323 |
| A | ASP327 |
| A | TYR394 |
| B | LYS320 |
| B | LEU321 |
| B | PHE322 |
| B | LEU323 |
| B | ASN324 |
| B | GLU325 |
| B | TYR394 |
| D | ARG317 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details |
| Chain | Residue |
| A | ARG317 |
| C | LYS320 |
| C | LEU321 |
| C | PHE322 |
| C | LEU323 |
| C | ASN324 |
| C | ASP327 |
| C | TYR394 |
| D | LYS320 |
| D | LEU321 |
| D | PHE322 |
| D | LEU323 |
| D | ASN324 |
| D | GLU325 |
| D | TYR394 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details |
| Chain | Residue |
| A | SER237 |
| A | HIS516 |
| A | ASP520 |
| C | SER237 |
| C | ASP520 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details |
| Chain | Residue |
| B | TYR530 |
| B | ASN532 |
| D | LEU434 |
| D | ALA435 |
| D | GLY437 |
| D | PRO450 |
| D | VAL453 |
| D | ARG454 |
| D | LEU457 |
| D | HOH670 |
| D | HOH692 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22049910, ECO:0000269|PubMed:22538822, ECO:0000305|PubMed:24451979, ECO:0007744|PDB:3CZD, ECO:0007744|PDB:3UNW, ECO:0007744|PDB:3VP0, ECO:0007744|PDB:3VP1 |
| Chain | Residue | Details |
| A | SER286 | |
| B | TYR414 | |
| B | TYR466 | |
| B | VAL484 | |
| C | SER286 | |
| C | ASN335 | |
| C | GLU381 | |
| C | TYR414 | |
| C | TYR466 | |
| C | VAL484 | |
| D | SER286 | |
| A | ASN335 | |
| D | ASN335 | |
| D | GLU381 | |
| D | TYR414 | |
| D | TYR466 | |
| D | VAL484 | |
| A | GLU381 | |
| A | TYR414 | |
| A | TYR466 | |
| A | VAL484 | |
| B | SER286 | |
| B | ASN335 | |
| B | GLU381 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22049910, ECO:0000269|PubMed:22538822, ECO:0000305|PubMed:24451979, ECO:0007744|PDB:3CZD, ECO:0007744|PDB:3UNW, ECO:0007744|PDB:3VP1 |
| Chain | Residue | Details |
| A | ASN388 | |
| B | ASN388 | |
| C | ASN388 | |
| D | ASN388 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | SITE: Cleavage; by MPP => ECO:0000250|UniProtKB:P13264 |
| Chain | Residue | Details |
| A | LEU72 | |
| B | LEU72 | |
| C | LEU72 | |
| D | LEU72 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:D3Z7P3 |
| Chain | Residue | Details |
| A | LYS130 | |
| A | LYS164 | |
| B | LYS130 | |
| B | LYS164 | |
| C | LYS130 | |
| C | LYS164 | |
| D | LYS130 | |
| D | LYS164 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | LYS311 | |
| B | LYS311 | |
| C | LYS311 | |
| D | LYS311 |
