4CQB
The reaction mechanism of the N-isopropylammelide isopropylaminohydrolase AtzC: insights from structural and mutagenesis studies
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 | 6 |
Details | BINDING SITE FOR RESIDUE ZN A 1404 |
Chain | Residue |
A | HIS60 |
A | HIS62 |
A | HIS217 |
A | ASP303 |
A | MLI1407 |
A | HOH2028 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN B 1404 |
Chain | Residue |
B | ASP303 |
B | MLI1408 |
B | HOH2037 |
B | HIS60 |
B | HIS62 |
B | HIS217 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL A 1405 |
Chain | Residue |
A | MET286 |
A | VAL288 |
A | ILE289 |
A | HOH2188 |
A | HOH2210 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL B 1405 |
Chain | Residue |
B | LYS42 |
B | ILE394 |
B | HOH2247 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE DMS B 1406 |
Chain | Residue |
A | HOH2215 |
B | TYR82 |
B | TRP251 |
B | ASP303 |
B | ASN304 |
B | TRP309 |
B | VAL310 |
B | MLI1408 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE DMS A 1406 |
Chain | Residue |
A | TYR82 |
A | HIS219 |
A | TRP251 |
A | ASP303 |
A | VAL310 |
A | MLI1407 |
A | HOH2181 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE DMS B 1407 |
Chain | Residue |
B | TYR227 |
B | ASN230 |
B | GLU263 |
site_id | AC8 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE MLI B 1408 |
Chain | Residue |
B | HIS62 |
B | LYS65 |
B | PHE158 |
B | GLN160 |
B | HIS217 |
B | HIS219 |
B | ASN304 |
B | TRP309 |
B | ZN1404 |
B | DMS1406 |
B | HOH2037 |
site_id | AC9 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE MLI A 1407 |
Chain | Residue |
A | HIS62 |
A | LYS65 |
A | GLN160 |
A | HIS217 |
A | HIS219 |
A | ASN304 |
A | TRP309 |
A | ZN1404 |
A | DMS1406 |
A | HOH2028 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MLI A 1408 |
Chain | Residue |
A | TYR227 |
A | ASN230 |
A | GLU263 |
A | HOH2176 |
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 |
A | HIS60 | |
A | HIS62 | |
A | HIS217 | |
A | ASP303 | |
B | HIS60 | |
B | HIS62 | |
B | HIS217 | |
B | ASP303 |