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7CNT

Structure of 2,5-dihydroxypridine Dioxygenase from Pseudomonas putida KT2440 in complex with product N-formylmaleamic acid formed via in crystallo reaction with 2,5-dihydroxypridine

Functional Information from GO Data
ChainGOidnamespacecontents
A0016491molecular_functionoxidoreductase activity
A0046872molecular_functionmetal ion binding
A0047075molecular_function2,5-dihydroxypyridine 5,6-dioxygenase activity
A1901848biological_processnicotinate catabolic process
B0016491molecular_functionoxidoreductase activity
B0046872molecular_functionmetal ion binding
B0047075molecular_function2,5-dihydroxypyridine 5,6-dioxygenase activity
B1901848biological_processnicotinate catabolic process
C0016491molecular_functionoxidoreductase activity
C0046872molecular_functionmetal ion binding
C0047075molecular_function2,5-dihydroxypyridine 5,6-dioxygenase activity
C1901848biological_processnicotinate catabolic process
D0016491molecular_functionoxidoreductase activity
D0046872molecular_functionmetal ion binding
D0047075molecular_function2,5-dihydroxypyridine 5,6-dioxygenase activity
D1901848biological_processnicotinate catabolic process
E0016491molecular_functionoxidoreductase activity
E0046872molecular_functionmetal ion binding
E0047075molecular_function2,5-dihydroxypyridine 5,6-dioxygenase activity
E1901848biological_processnicotinate catabolic process
F0016491molecular_functionoxidoreductase activity
F0046872molecular_functionmetal ion binding
F0047075molecular_function2,5-dihydroxypyridine 5,6-dioxygenase activity
F1901848biological_processnicotinate catabolic process
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

250359

PDB entries from 2026-03-11

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