5AKQ
X-ray structure and mutagenesis studies of the N-isopropylammelide isopropylaminohydrolase, AtzC
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| A | 0016814 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines |
| A | 0018764 | molecular_function | N-isopropylammelide isopropylaminohydrolase activity |
| A | 0019381 | biological_process | atrazine catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| B | 0016814 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines |
| B | 0018764 | molecular_function | N-isopropylammelide isopropylaminohydrolase activity |
| B | 0019381 | biological_process | atrazine catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 1404 |
| Chain | Residue |
| A | VAL196 |
| A | VAL196 |
| A | GLU197 |
| A | GLU197 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 1404 |
| Chain | Residue |
| B | VAL196 |
| B | VAL196 |
| B | GLU197 |
| B | GLU197 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 1405 |
| Chain | Residue |
| B | HIS62 |
| B | HIS217 |
| B | HIS249 |
| B | ASP303 |
| B | HIS60 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 1405 |
| Chain | Residue |
| A | HIS60 |
| A | HIS62 |
| A | HIS217 |
| A | ASP303 |
Functional Information from PROSITE/UniProt
| site_id | PS01137 |
| Number of Residues | 9 |
| Details | TATD_1 TatD deoxyribonuclease family signature 1. FVDAHtHMD |
| Chain | Residue | Details |
| A | PHE56-ASP64 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:26390431 |
| Chain | Residue | Details |
| A | HIS249 | |
| B | HIS249 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:26390431, ECO:0000269|Ref.3 |
| Chain | Residue | Details |
| B | HIS217 | |
| B | ASP303 | |
| A | HIS60 | |
| A | HIS62 | |
| A | HIS217 | |
| A | ASP303 | |
| B | HIS60 | |
| B | HIS62 |
