4MUZ
Crystal structure of orotidine 5'-monophosphate decarboxylase from Archaeoglobus fulgidus complexed with inhibitor BMP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004590 | molecular_function | orotidine-5'-phosphate decarboxylase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
| A | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016831 | molecular_function | carboxy-lyase activity |
| A | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
| B | 0004590 | molecular_function | orotidine-5'-phosphate decarboxylase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
| B | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016831 | molecular_function | carboxy-lyase activity |
| B | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE BMP A 301 |
| Chain | Residue |
| A | ASP29 |
| A | GLY207 |
| A | ARG208 |
| A | HOH401 |
| A | HOH403 |
| A | HOH405 |
| A | HOH413 |
| A | HOH415 |
| B | ASP82 |
| B | VAL83 |
| B | THR86 |
| A | LYS51 |
| A | ASN53 |
| A | ASP77 |
| A | LYS79 |
| A | LEU133 |
| A | SER134 |
| A | PRO186 |
| A | GLN191 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 302 |
| Chain | Residue |
| A | SER135 |
| A | GLN191 |
| A | ARG208 |
| A | HOH426 |
| A | HOH550 |
| B | PRO84 |
| B | TYR85 |
| site_id | AC3 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE BMP B 301 |
| Chain | Residue |
| A | ASP82 |
| A | VAL83 |
| A | THR86 |
| B | ASP29 |
| B | LYS51 |
| B | ASN53 |
| B | ASP77 |
| B | LYS79 |
| B | LEU133 |
| B | SER134 |
| B | PRO186 |
| B | GLN191 |
| B | GLY207 |
| B | ARG208 |
| B | HOH401 |
| B | HOH402 |
| B | HOH404 |
| B | HOH409 |
| B | HOH411 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 302 |
| Chain | Residue |
| A | VAL83 |
| A | PRO84 |
| A | TYR85 |
| B | SER135 |
| B | GLN191 |
| B | ARG208 |
| B | HOH421 |
| B | HOH582 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_01200","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 48 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01200","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
