The Crystal Structure of Human Porphobilinogen Deaminase at 2.8A resolution

3-[5-{[3-(2-carboxyethyl)-4-(carboxymethyl)-5-methyl-1H-pyrrol-2-yl]methyl}-4-(carboxymethyl)-1H-pyrrol-3-yl]propanoic acid

Structure of human porphobilinogen deaminase at 2.8 A: the molecular basis of acute intermittent porphyria

PBG-D, Pre-uroporphyrinogen synthase, Hydroxymethylbilane synthase, HMBS

MSGNGNAAATAEENSPKMRVIRVGTRKSQLARIQTDSVVATLKASYPGLQFEIIAMSTTGDKILDTALSKIGEKSLFTKE
LEHALEKNEVDLVVHSLKDLPTVLPPGFTIGAICKRENPHDAVVFHPKFVGKTLETLPEKSVVGTSSLRRAAQLQRKFPH
LEFRSIQGNLNTRLRKLDEQQEFSAIILATAGLQRMGWHNRVGQILHPEECMYAVGQGALGVEVRAKDQDILDLVGVLHD
PETLLRCIAERAFLRHLEGGCSVPVAVHTAMKDGQLYLTGGVWSLDGSDSIQETMQATIHVPAQHEDGPEDDPQLVGITA
RNIPRGPQLAAQNLGISLANLLLSKGAKNILDVARQLNDAH

0.6M ammonium sulphate, 1.2M lithium sulphate, 5% (v/v) ethylene glycol, 50mM sodium citrate, 50mM DTT, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K

ALPHA AND BETA PROTEIN, Alternative splicing, Cytoplasm, Disease mutation, Heme biosynthesis, Porphyrin biosynthesis, Transferase

chain A and (resseq 20:55 or resseq 88:299 or resseq 312:355 )

chain B and (resseq 20:55 or resseq 88:299 or resseq 312:355 or resseq 20:55 or resseq 88:299 or resseq 312:355 )

MSGNGNAAATAEENSPKMRVIRVGTRKSQLARIQTDSVVATLKASYPGLQFEIIAMSTTGDKILDTALSKIGEKSLFTKE
LEHALEKNEVDLVVHSLKDLPTVLPPGFTIGAICKRENPHDAVVFHPKFVGKTLETLPEKSVVGTSSLRRAAQLQRKFPH
LEFRSIRGNLNTRLRKLDEQQEFSAIILATAGLQRMGWHNRVGQILHPEECMYAVGQGALGVEVRAKDQDILDLVGVLHD
PETLLRCIAERAFLRHLEGGCSVPVAVHTAMKDGQLYLTGGVWSLDGSDSIQETMQATIHVPAQHEDGPEDDPQLVGITA
RNIPRGPQLAAQNLGISLANLLLSKGAKNILDVARQLNDAH