Table 3. Alignment of murine and human pyridoxal 5’-phosphate phosphatase (PDXP) structures.
7,8-DHF-mPDXP (+P), protomer A | 7,8-DHF-mPDXP (– P), protomer B | |
---|---|---|
7,8-DHF-mPDXP (+P), protomer B | 0.43 Å | |
Apo-mPDXP, protomer A | 0.50 Å | 0.71 Å |
Apo-mPDXP, protomer B | 0.60 Å | 0.69 Å |
7,8-DHF-hPDXP (+P) | 7,8-DHF-hPDXP (–P) | |
7,8-DHF-hPDXP (–P) | 0.37 Å | |
Apo-hPDXP | 0.54 Å | 0.45 Å |
PLP-hPDXP | 0.39 Å | 0.29 Å |
Cα atom-based alignment of the structures representing murine apo-PDXP (PDB: 4BX3), 7,8-dihydroxyflavone (7,8-DHF)-bound murine PDXP (with inhibitor-bound protomer A and inhibitor-free protomer B; PDB: 8QFW), human apo-PDXP (PDB: 2P27), 7,8-DHF-bound human PDXP with phosphate (+P) (PDB: 9EM1), 7,8-DHF-bound human PDXP without phosphate (–P) (PDB: 8S8A) and pyridoxal 5’-phosphate (PLP)-bound human PDXP (PDB: 2CFT); mPDXP, murine PDXP; hPDXP, human PDXP. Root mean square deviations are indicated.