7P7N
X-RAY CRYSTAL STRUCTURE OF SPOROSARCINA PASTEURII UREASE INHIBITED BY THE GOLD(I)-PHOSPHINE COMPOUND Au(PEt3)I DETERMINED AT 1.80 ANGSTROMS
This is a non-PDB format compatible entry.
Functional Information from GO Data
Chain | GOid | namespace | contents |
AAA | 0005737 | cellular_component | cytoplasm |
AAA | 0009039 | molecular_function | urease activity |
AAA | 0016151 | molecular_function | nickel cation binding |
AAA | 0016787 | molecular_function | hydrolase activity |
AAA | 0019627 | biological_process | urea metabolic process |
AAA | 0043419 | biological_process | urea catabolic process |
BBB | 0005737 | cellular_component | cytoplasm |
BBB | 0009039 | molecular_function | urease activity |
BBB | 0016787 | molecular_function | hydrolase activity |
BBB | 0035550 | cellular_component | urease complex |
BBB | 0043419 | biological_process | urea catabolic process |
CCC | 0005737 | cellular_component | cytoplasm |
CCC | 0009039 | molecular_function | urease activity |
CCC | 0016151 | molecular_function | nickel cation binding |
CCC | 0016787 | molecular_function | hydrolase activity |
CCC | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
CCC | 0043419 | biological_process | urea catabolic process |
CCC | 0046872 | molecular_function | metal ion binding |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor => ECO:0000305 |
Chain | Residue | Details |
CCC | HIS324 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01953, ECO:0000269|PubMed:10368287, ECO:0000269|PubMed:10766443, ECO:0000269|PubMed:11713685, ECO:0000269|PubMed:15038715, ECO:0000269|PubMed:30969470, ECO:0000269|DOI:10.1007/s007750050231 |
Chain | Residue | Details |
CCC | VAL138 | |
CCC | VAL276 | |
CCC | ALA364 |
site_id | SWS_FT_FI3 |
Number of Residues | 5 |
Details | BINDING: BINDING => ECO:0000269|PubMed:30969470 |
Chain | Residue | Details |
CCC | PHE140 | |
CCC | THR171 | |
CCC | GLU223 | |
CCC | SER250 | |
CCC | MET367 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | BINDING: via carbamate group => ECO:0000255|HAMAP-Rule:MF_01953, ECO:0000269|PubMed:10368287, ECO:0000269|PubMed:10766443, ECO:0000269|PubMed:11713685, ECO:0000269|PubMed:15038715, ECO:0000269|PubMed:30969470, ECO:0000269|DOI:10.1007/s007750050231 |
Chain | Residue | Details |
CCC | ILE221 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: N6-carboxylysine => ECO:0000255|HAMAP-Rule:MF_01953, ECO:0000269|PubMed:10368287, ECO:0000269|PubMed:10766443, ECO:0000269|PubMed:11713685, ECO:0000269|PubMed:15038715, ECO:0000269|PubMed:30969470, ECO:0000269|DOI:10.1007/s007750050231, ECO:0007744|PDB:1IE7, ECO:0007744|PDB:1S3T, ECO:0007744|PDB:1UBP, ECO:0007744|PDB:2UBP, ECO:0007744|PDB:4UBP |
Chain | Residue | Details |
CCC | ILE221 |