6UMC
Crystal structure of human GAC in complex with inhibitor UPGL00012
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 | 38 |
Details | binding site for Di-peptide U27 A 601 and ARG D 317 |
Chain | Residue |
A | GLY315 |
A | LEU323 |
A | ASN324 |
A | GLU325 |
A | TYR394 |
B | LYS320 |
B | LEU321 |
B | PHE322 |
B | LEU323 |
B | GLU325 |
B | TYR394 |
A | LEU316 |
C | ARG317 |
C | LYS320 |
C | LEU321 |
C | PHE322 |
C | LEU323 |
C | GLU325 |
C | TYR394 |
D | GLY315 |
D | LEU316 |
D | PHE318 |
A | PHE318 |
D | PHE318 |
D | ASN319 |
D | LYS320 |
D | LEU321 |
D | PHE322 |
D | LEU323 |
D | ASN324 |
D | GLU325 |
D | TYR394 |
A | ASN319 |
A | LYS320 |
A | LYS320 |
A | LEU321 |
A | LEU321 |
A | PHE322 |
site_id | AC2 |
Number of Residues | 17 |
Details | binding site for Di-peptide U27 D 601 and LYS D 320 |
Chain | Residue |
B | LYS320 |
B | LEU321 |
B | PHE322 |
B | LEU323 |
B | GLU325 |
B | TYR394 |
C | ARG317 |
D | PHE318 |
D | PHE318 |
D | ASN319 |
D | LEU321 |
D | LEU321 |
D | PHE322 |
D | LEU323 |
D | ASN324 |
D | GLU325 |
D | TYR394 |
site_id | AC3 |
Number of Residues | 17 |
Details | binding site for Di-peptide U27 D 601 and LYS D 320 |
Chain | Residue |
B | LYS320 |
B | LEU321 |
B | PHE322 |
B | LEU323 |
B | GLU325 |
B | TYR394 |
C | ARG317 |
D | PHE318 |
D | PHE318 |
D | ASN319 |
D | LEU321 |
D | LEU321 |
D | PHE322 |
D | LEU323 |
D | ASN324 |
D | GLU325 |
D | TYR394 |
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 |