##gff-version 3 P07742 UniProtKB Chain 1 792 . . . ID=PRO_0000187191;Note=Ribonucleoside-diphosphate reductase large subunit P07742 UniProtKB Domain 1 92 . . . Note=ATP-cone;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00492 P07742 UniProtKB Active site 427 427 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 P07742 UniProtKB Active site 429 429 . . . Note=Cysteine radical intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250 P07742 UniProtKB Active site 431 431 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 P07742 UniProtKB Binding site 5 6 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23921 P07742 UniProtKB Binding site 11 17 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23921 P07742 UniProtKB Binding site 53 53 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23921 P07742 UniProtKB Binding site 57 57 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23921 P07742 UniProtKB Binding site 202 202 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23921 P07742 UniProtKB Binding site 217 217 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23921 P07742 UniProtKB Binding site 226 228 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23921 P07742 UniProtKB Binding site 243 243 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23921 P07742 UniProtKB Binding site 256 256 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23921 P07742 UniProtKB Binding site 263 264 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23921 P07742 UniProtKB Binding site 427 427 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23921 P07742 UniProtKB Binding site 431 431 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23921 P07742 UniProtKB Binding site 604 607 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23921 P07742 UniProtKB Site 218 218 . . . Note=Important for hydrogen atom transfer;Ontology_term=ECO:0000250;evidence=ECO:0000250 P07742 UniProtKB Site 444 444 . . . Note=Important for hydrogen atom transfer;Ontology_term=ECO:0000250;evidence=ECO:0000250 P07742 UniProtKB Site 737 737 . . . Note=Important for electron transfer;Ontology_term=ECO:0000250;evidence=ECO:0000250 P07742 UniProtKB Site 738 738 . . . Note=Important for electron transfer;Ontology_term=ECO:0000250;evidence=ECO:0000250 P07742 UniProtKB Site 787 787 . . . Note=Interacts with thioredoxin/glutaredoxin;Ontology_term=ECO:0000250;evidence=ECO:0000250 P07742 UniProtKB Site 790 790 . . . Note=Interacts with thioredoxin/glutaredoxin;Ontology_term=ECO:0000250;evidence=ECO:0000250 P07742 UniProtKB Modified residue 17 17 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23921 P07742 UniProtKB Modified residue 376 376 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23921 P07742 UniProtKB Modified residue 751 751 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23921 P07742 UniProtKB Disulfide bond 218 444 . . . Note=Redox-active;Ontology_term=ECO:0000250;evidence=ECO:0000250 P07742 UniProtKB Sequence conflict 202 202 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305