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 | 28 |
| Details | Region: {"description":"Highly mobile activation loop","evidences":[{"source":"UniProtKB","id":"D3Z7P3","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22049910","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22538822","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24451979","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3CZD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UNW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3VP0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3VP1","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22049910","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22538822","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24451979","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3CZD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UNW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3VP1","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"D3Z7P3","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
