2AQ6
X-ray crystal structure of mycobacterium tuberculosis pyridoxine 5'-phosphate oxidase complexed with pyridoxal 5'-phosphate at 1.7 a resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0010181 | molecular_function | FMN binding |
| A | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0042816 | biological_process | vitamin B6 metabolic process |
| A | 0070402 | molecular_function | NADPH binding |
| A | 0070967 | molecular_function | coenzyme F420 binding |
| A | 0071949 | molecular_function | FAD binding |
| B | 0010181 | molecular_function | FMN binding |
| B | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0042816 | biological_process | vitamin B6 metabolic process |
| B | 0070402 | molecular_function | NADPH binding |
| B | 0070967 | molecular_function | coenzyme F420 binding |
| B | 0071949 | molecular_function | FAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PLP A 401 |
| Chain | Residue |
| A | SER34 |
| A | HOH552 |
| B | TYR79 |
| A | ASN35 |
| A | ARG55 |
| A | LYS57 |
| A | ARG129 |
| A | HOH477 |
| A | HOH489 |
| A | HOH529 |
| A | HOH544 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"25644473","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25644473","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |






