4P5A
Crystal structure of a UMP/dUMP methylase PolB from Streptomyces cacaoi bound with 5-Br UMP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004799 | molecular_function | thymidylate synthase activity |
| A | 0006231 | biological_process | dTMP biosynthetic process |
| A | 0006235 | biological_process | dTTP biosynthetic process |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0009165 | biological_process | nucleotide biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0032259 | biological_process | methylation |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0050797 | molecular_function | thymidylate synthase (FAD) activity |
| A | 0070402 | molecular_function | NADPH binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004799 | molecular_function | thymidylate synthase activity |
| B | 0006231 | biological_process | dTMP biosynthetic process |
| B | 0006235 | biological_process | dTTP biosynthetic process |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0009165 | biological_process | nucleotide biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0032259 | biological_process | methylation |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0050797 | molecular_function | thymidylate synthase (FAD) activity |
| B | 0070402 | molecular_function | NADPH binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004799 | molecular_function | thymidylate synthase activity |
| C | 0006231 | biological_process | dTMP biosynthetic process |
| C | 0006235 | biological_process | dTTP biosynthetic process |
| C | 0008168 | molecular_function | methyltransferase activity |
| C | 0009165 | biological_process | nucleotide biosynthetic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0032259 | biological_process | methylation |
| C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| C | 0050797 | molecular_function | thymidylate synthase (FAD) activity |
| C | 0070402 | molecular_function | NADPH binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0004799 | molecular_function | thymidylate synthase activity |
| D | 0006231 | biological_process | dTMP biosynthetic process |
| D | 0006235 | biological_process | dTTP biosynthetic process |
| D | 0008168 | molecular_function | methyltransferase activity |
| D | 0009165 | biological_process | nucleotide biosynthetic process |
| D | 0016740 | molecular_function | transferase activity |
| D | 0032259 | biological_process | methylation |
| D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| D | 0050797 | molecular_function | thymidylate synthase (FAD) activity |
| D | 0070402 | molecular_function | NADPH binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 32 |
| Details | binding site for residue FAD A 301 |
| Chain | Residue |
| A | ARG86 |
| A | HOH445 |
| A | HOH448 |
| A | HOH466 |
| A | HOH467 |
| A | HOH551 |
| A | HOH577 |
| A | HOH578 |
| A | HOH579 |
| A | HOH580 |
| B | ASN93 |
| A | HIS87 |
| B | GLU94 |
| B | SER96 |
| B | 5BU301 |
| B | HOH493 |
| C | HIS61 |
| C | SER63 |
| C | GLU66 |
| C | THR89 |
| C | ASN182 |
| C | ARG184 |
| A | ARG88 |
| C | FAD301 |
| C | HOH454 |
| C | HOH546 |
| A | THR89 |
| A | HIS188 |
| A | LEU192 |
| A | ARG193 |
| A | HIS204 |
| A | HOH422 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | binding site for residue 5BU A 302 |
| Chain | Residue |
| A | MET85 |
| A | GLU94 |
| A | GLU95 |
| A | SER96 |
| A | ALA97 |
| A | ARG98 |
| A | ARG166 |
| A | HOH427 |
| A | HOH442 |
| A | HOH453 |
| B | ARG82 |
| B | HIS83 |
| B | ARG86 |
| B | TYR124 |
| B | ARG193 |
| B | FAD302 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | binding site for residue 5BU B 301 |
| Chain | Residue |
| A | ARG82 |
| A | HIS83 |
| A | ARG86 |
| A | TYR124 |
| A | ARG193 |
| A | FAD301 |
| B | GLU94 |
| B | GLU95 |
| B | SER96 |
| B | ALA97 |
| B | ARG98 |
| B | ARG166 |
| B | HOH446 |
| B | HOH479 |
| B | HOH514 |
| site_id | AC4 |
| Number of Residues | 31 |
| Details | binding site for residue FAD B 302 |
| Chain | Residue |
| A | ASN93 |
| A | GLU94 |
| A | 5BU302 |
| A | HOH462 |
| B | ARG86 |
| B | HIS87 |
| B | ARG88 |
| B | THR89 |
| B | HIS188 |
| B | LEU192 |
| B | ARG193 |
| B | HIS204 |
| B | HOH455 |
| B | HOH465 |
| B | HOH467 |
| B | HOH471 |
| B | HOH477 |
| B | HOH498 |
| B | HOH499 |
| B | HOH517 |
| B | HOH534 |
| B | HOH559 |
| D | HIS61 |
| D | SER63 |
| D | GLU66 |
| D | ASN182 |
| D | ARG184 |
| D | FAD302 |
| D | HOH420 |
| D | HOH482 |
| D | HOH527 |
| site_id | AC5 |
| Number of Residues | 32 |
| Details | binding site for residue FAD C 301 |
| Chain | Residue |
| A | ARG184 |
| A | FAD301 |
| A | HOH551 |
| A | HOH552 |
| C | ARG86 |
| C | HIS87 |
| C | ARG88 |
| C | THR89 |
| C | HIS188 |
| C | LEU192 |
| C | ARG193 |
| C | HIS204 |
| C | HOH452 |
| C | HOH460 |
| C | HOH471 |
| C | HOH480 |
| C | HOH490 |
| C | HOH491 |
| C | HOH507 |
| C | HOH508 |
| C | HOH543 |
| C | HOH544 |
| C | HOH548 |
| C | HOH585 |
| D | ASN93 |
| D | GLU94 |
| D | 5BU301 |
| A | HIS61 |
| A | SER63 |
| A | GLU66 |
| A | THR89 |
| A | ASN182 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | binding site for residue 5BU C 302 |
| Chain | Residue |
| C | GLU94 |
| C | GLU95 |
| C | SER96 |
| C | ALA97 |
| C | ARG98 |
| C | ARG166 |
| C | HOH442 |
| C | HOH467 |
| C | HOH498 |
| D | ARG82 |
| D | HIS83 |
| D | ARG86 |
| D | TYR124 |
| D | ARG193 |
| D | FAD302 |
| site_id | AC7 |
| Number of Residues | 15 |
| Details | binding site for residue 5BU D 301 |
| Chain | Residue |
| C | ARG82 |
| C | HIS83 |
| C | ARG86 |
| C | TYR124 |
| C | ARG193 |
| C | FAD301 |
| D | MET85 |
| D | GLU94 |
| D | GLU95 |
| D | SER96 |
| D | ALA97 |
| D | ARG98 |
| D | ARG166 |
| D | HOH422 |
| D | HOH493 |
| site_id | AC8 |
| Number of Residues | 27 |
| Details | binding site for residue FAD D 302 |
| Chain | Residue |
| B | HIS61 |
| B | SER63 |
| B | GLU66 |
| B | THR89 |
| B | ASN182 |
| B | ARG184 |
| B | FAD302 |
| B | HOH517 |
| C | ASN93 |
| C | GLU94 |
| C | 5BU302 |
| C | HOH557 |
| D | ARG86 |
| D | HIS87 |
| D | ARG88 |
| D | THR89 |
| D | HIS188 |
| D | LEU192 |
| D | ARG193 |
| D | HOH442 |
| D | HOH444 |
| D | HOH445 |
| D | HOH458 |
| D | HOH462 |
| D | HOH466 |
| D | HOH519 |
| D | HOH527 |
