6H6X
Structure of an evolved dimeric form of the UbiD-class enzyme HmfF from Pelotomaculum thermopropionicum in complex with prFMN
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006744 | biological_process | ubiquinone biosynthetic process |
| A | 0008694 | molecular_function | 4-hydroxy-3-polyprenylbenzoate decarboxylase activity |
| A | 0009636 | biological_process | response to toxic substance |
| A | 0016831 | molecular_function | carboxy-lyase activity |
| A | 0018799 | molecular_function | 4-hydroxybenzoate decarboxylase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006744 | biological_process | ubiquinone biosynthetic process |
| B | 0008694 | molecular_function | 4-hydroxy-3-polyprenylbenzoate decarboxylase activity |
| B | 0009636 | biological_process | response to toxic substance |
| B | 0016831 | molecular_function | carboxy-lyase activity |
| B | 0018799 | molecular_function | 4-hydroxybenzoate decarboxylase activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue K B 501 |
| Chain | Residue |
| B | VAL148 |
| B | SER200 |
| B | ALA202 |
| B | GLU210 |
| B | 4LU503 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue MN B 502 |
| Chain | Residue |
| B | HOH603 |
| B | HOH613 |
| B | ASN147 |
| B | HIS169 |
| B | GLU210 |
| B | 4LU503 |
| site_id | AC3 |
| Number of Residues | 22 |
| Details | binding site for residue 4LU B 503 |
| Chain | Residue |
| B | THR132 |
| B | ASN147 |
| B | VAL148 |
| B | SER149 |
| B | ILE150 |
| B | HIS151 |
| B | ARG152 |
| B | LEU164 |
| B | LEU166 |
| B | ARG168 |
| B | HIS169 |
| B | SER200 |
| B | GLN201 |
| B | GLU210 |
| B | GLU259 |
| B | HIS296 |
| B | K501 |
| B | MN502 |
| B | HOH601 |
| B | HOH613 |
| B | HOH628 |
| B | HOH652 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 504 |
| Chain | Residue |
| B | ARG385 |
| B | ARG390 |
| B | ASP391 |
| B | ASP418 |
| B | THR420 |
| B | HOH696 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue K A 501 |
| Chain | Residue |
| A | VAL148 |
| A | SER200 |
| A | ALA202 |
| A | GLU210 |
| A | 4LU503 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue MN A 502 |
| Chain | Residue |
| A | ASN147 |
| A | HIS169 |
| A | GLU210 |
| A | 4LU503 |
| A | HOH633 |
| site_id | AC7 |
| Number of Residues | 20 |
| Details | binding site for residue 4LU A 503 |
| Chain | Residue |
| A | THR132 |
| A | ASN147 |
| A | SER149 |
| A | ILE150 |
| A | HIS151 |
| A | ARG152 |
| A | LEU164 |
| A | LEU166 |
| A | ARG168 |
| A | HIS169 |
| A | SER200 |
| A | GLN201 |
| A | GLU210 |
| A | GLU259 |
| A | HIS296 |
| A | K501 |
| A | MN502 |
| A | HOH601 |
| A | HOH633 |
| A | HOH640 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 504 |
| Chain | Residue |
| A | ARG385 |
| A | ARG390 |
| A | ASP391 |
| A | ASP418 |
| A | THR420 |
| A | HOH656 |
