3MJM
His257Ala mutant of dihydroorotase from E. coli
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004151 | molecular_function | dihydroorotase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
| A | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016812 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides |
| A | 0019856 | biological_process | pyrimidine nucleobase biosynthetic process |
| A | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004151 | molecular_function | dihydroorotase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
| B | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016812 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides |
| B | 0019856 | biological_process | pyrimidine nucleobase biosynthetic process |
| 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 | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 400 |
| Chain | Residue |
| A | KCX102 |
| A | HIS139 |
| A | HIS177 |
| A | ZN401 |
| A | HOH453 |
| A | DOR1410 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 401 |
| Chain | Residue |
| A | ASP250 |
| A | ZN400 |
| A | HOH453 |
| A | HIS16 |
| A | HIS18 |
| A | KCX102 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE DOR A 1410 |
| Chain | Residue |
| A | HIS18 |
| A | ARG20 |
| A | ASN44 |
| A | HIS139 |
| A | CYS221 |
| A | LEU222 |
| A | ASP250 |
| A | ALA252 |
| A | HIS254 |
| A | ALA266 |
| A | GLY267 |
| A | ZN400 |
| A | HOH453 |
| A | HOH496 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 400 |
| Chain | Residue |
| B | KCX102 |
| B | HIS139 |
| B | HIS177 |
| B | NCD2410 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 401 |
| Chain | Residue |
| B | HIS16 |
| B | HIS18 |
| B | KCX102 |
| B | ASP250 |
| B | NCD2410 |
| site_id | AC6 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE NCD B 2410 |
| Chain | Residue |
| B | HIS18 |
| B | ARG20 |
| B | ASN44 |
| B | KCX102 |
| B | THR109 |
| B | THR110 |
| B | HIS139 |
| B | HIS177 |
| B | CYS221 |
| B | LEU222 |
| B | ASP250 |
| B | ALA252 |
| B | HIS254 |
| B | ALA266 |
| B | GLY267 |
| B | ZN400 |
| B | ZN401 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE CP B 348 |
| Chain | Residue |
| A | PHE150 |
| A | ARG207 |
| A | ARG227 |
| A | HOH592 |
| B | PHE150 |
| B | ARG207 |
| B | ARG227 |
| B | HOH352 |
| B | HOH517 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00219","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00219","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"APR-2010","submissionDatabase":"PDB data bank","title":"His257Ala mutant of dihydroorotase from E. coli.","authors":["Ernberg K.E.","Lee M.","Christopherson R.I.","Maher M.J.","Guss J.M."]}},{"source":"PDB","id":"3MJM","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00219","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"APR-2010","submissionDatabase":"PDB data bank","title":"His257Ala mutant of dihydroorotase from E. coli.","authors":["Ernberg K.E.","Lee M.","Christopherson R.I.","Maher M.J.","Guss J.M."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"via carbamate group","evidences":[{"source":"HAMAP-Rule","id":"MF_00219","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"APR-2010","submissionDatabase":"PDB data bank","title":"His257Ala mutant of dihydroorotase from E. coli.","authors":["Ernberg K.E.","Lee M.","Christopherson R.I.","Maher M.J.","Guss J.M."]}},{"source":"PDB","id":"3MJM","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"HAMAP-Rule","id":"MF_00219","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
