3MPG
Dihydroorotase from Bacillus anthracis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004038 | molecular_function | allantoinase activity |
| A | 0004151 | molecular_function | dihydroorotase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006145 | biological_process | purine nucleobase catabolic process |
| A | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| A | 0008270 | molecular_function | zinc ion binding |
| 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 | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004038 | molecular_function | allantoinase activity |
| B | 0004151 | molecular_function | dihydroorotase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006145 | biological_process | purine nucleobase catabolic process |
| B | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| B | 0008270 | molecular_function | zinc ion binding |
| 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 | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 429 |
| Chain | Residue |
| A | HIS59 |
| A | HIS61 |
| A | ASP151 |
| A | ASP304 |
| A | ZN430 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 430 |
| Chain | Residue |
| A | ASP151 |
| A | HIS178 |
| A | HIS231 |
| A | ZN429 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 429 |
| Chain | Residue |
| B | HIS59 |
| B | HIS61 |
| B | ASP151 |
| B | ASP304 |
| B | ZN430 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 430 |
| Chain | Residue |
| B | ASP151 |
| B | HIS178 |
| B | HIS231 |
| B | ZN429 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00220, ECO:0000305|PubMed:27499369 |
| Chain | Residue | Details |
| A | ASP304 | |
| B | ASP304 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00220, ECO:0000269|PubMed:21045288, ECO:0000269|PubMed:27499369, ECO:0007744|PDB:3MPG, ECO:0007744|PDB:4YIW |
| Chain | Residue | Details |
| A | HIS59 | |
| B | HIS178 | |
| B | HIS231 | |
| B | ASP304 | |
| A | HIS61 | |
| A | ASP151 | |
| A | HIS178 | |
| A | HIS231 | |
| A | ASP304 | |
| B | HIS59 | |
| B | HIS61 | |
| B | ASP151 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00220, ECO:0000305|PubMed:27499369 |
| Chain | Residue | Details |
| A | ASN93 | |
| A | ASN277 | |
| A | HIS308 | |
| A | PHE322 | |
| B | ASN93 | |
| B | ASN277 | |
| B | HIS308 | |
| B | PHE322 |
