3MJM
His257Ala mutant of dihydroorotase from E. coli
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004151 | molecular_function | dihydroorotase activity |
| 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 | 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 | ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00219 |
| Chain | Residue | Details |
| A | ASP250 | |
| B | ASP250 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000269|Ref.2, ECO:0007744|PDB:3MJM |
| Chain | Residue | Details |
| A | HIS16 | |
| B | ASP250 | |
| A | HIS18 | |
| A | HIS139 | |
| A | HIS177 | |
| A | ASP250 | |
| B | HIS16 | |
| B | HIS18 | |
| B | HIS139 | |
| B | HIS177 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000305|Ref.2 |
| Chain | Residue | Details |
| A | ASN44 | |
| A | LEU222 | |
| A | HIS254 | |
| A | ALA266 | |
| B | ASN44 | |
| B | LEU222 | |
| B | HIS254 | |
| B | ALA266 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: via carbamate group => ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000269|Ref.2, ECO:0007744|PDB:3MJM |
| Chain | Residue | Details |
| A | KCX102 | |
| B | KCX102 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-carboxylysine => ECO:0000255|HAMAP-Rule:MF_00219 |
| Chain | Residue | Details |
| A | KCX102 | |
| B | KCX102 |
