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 | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"26390431","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26390431","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"AUG-2007","submissionDatabase":"PDB data bank","title":"Crystal structure of N-isopropylammelide isopropylaminohydrolase AtzC from Pseudomonas sp. strain ADP complexed with Zn.","authors":["Fedorov A.A.","Fedorov E.V.","Seffernick J.","Wackett L.P.","Burley S.K.","Almo S.C."]}}]} |
| Chain | Residue | Details |
