3VP1
Crystal structure of human glutaminase in complex with L-glutamate and BPTES
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE 04A A 601 |
Chain | Residue |
A | ARG317 |
A | ARG317 |
A | PHE318 |
A | LYS320 |
A | PHE322 |
A | PHE322 |
A | LEU323 |
A | ASN324 |
A | TYR394 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GLU A 602 |
Chain | Residue |
A | TYR249 |
A | GLN285 |
A | SER286 |
A | ASN335 |
A | GLU381 |
A | ASN388 |
A | TYR414 |
A | TYR466 |
A | VAL484 |
site_id | AC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SO4 A 603 |
Chain | Residue |
A | PHE373 |
A | SER374 |
A | ASN375 |
A | ASN375 |
A | ALA376 |
A | ALA376 |
A | HOH726 |
A | HOH726 |
A | HOH762 |
A | HOH762 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 604 |
Chain | Residue |
A | LYS320 |
A | ARG387 |
A | TYR394 |
A | LYS398 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
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 | |
A | ASN335 | |
A | GLU381 | |
A | TYR414 | |
A | TYR466 | |
A | VAL484 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
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 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
A | LYS311 |