6KLK
Crystal structure of the Pseudomonas aeruginosa dihydropyrimidinase complexed with 5-FU
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004157 | molecular_function | dihydropyrimidinase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
A | 0016812 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides |
A | 0046872 | molecular_function | metal ion binding |
B | 0004157 | molecular_function | dihydropyrimidinase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
B | 0016812 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 12 |
Details | binding site for residue URF A 501 |
Chain | Residue |
A | HIS61 |
A | ASN337 |
A | ZN502 |
A | ZN503 |
A | LEU64 |
A | KCX150 |
A | PHE152 |
A | TYR155 |
A | MET288 |
A | SER289 |
A | ASP316 |
A | CYS318 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue ZN A 502 |
Chain | Residue |
A | HIS59 |
A | HIS61 |
A | KCX150 |
A | ASP316 |
A | URF501 |
A | ZN503 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue ZN A 503 |
Chain | Residue |
A | KCX150 |
A | HIS183 |
A | HIS239 |
A | URF501 |
A | ZN502 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue ZN B 501 |
Chain | Residue |
B | HIS59 |
B | HIS61 |
B | KCX150 |
B | ASP316 |
B | ZN502 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue ZN B 502 |
Chain | Residue |
B | KCX150 |
B | HIS183 |
B | HIS239 |
B | ZN501 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q9P903 |
Chain | Residue | Details |
A | HIS59 | |
B | HIS61 | |
B | TYR155 | |
B | HIS183 | |
B | HIS239 | |
B | SER289 | |
B | ASP316 | |
B | ASN337 | |
A | HIS61 | |
A | TYR155 | |
A | HIS183 | |
A | HIS239 | |
A | SER289 | |
A | ASP316 | |
A | ASN337 | |
B | HIS59 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: via carbamate group => ECO:0000250|UniProtKB:Q9P903 |
Chain | Residue | Details |
A | KCX150 | |
B | KCX150 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: N6-carboxylysine => ECO:0000250|UniProtKB:Q9P903 |
Chain | Residue | Details |
A | KCX150 | |
B | KCX150 |