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. 2024 Jun 10;13:RP93094. doi: 10.7554/eLife.93094

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.