eF-site ID 5m6r-B PDB Code 5m6r Chain B click to enlarge Title Human porphobilinogen deaminase in complex with reaction intermediate Classification TRANSFERASE Compound Porphobilinogen deaminase Source (HEM3_HUMAN) Sequence B:  MRVIRVGTRKSQLARIQTDSVVATLKASYPGLQFEIIAMS TTGDLFTKELEHALEKNEVDLVVHSLKDLPTVLPPGFTIG AICKRENPHDAVVFHPKFVGKTLETLPEKSVVGTSSLRRA AQLQRKFPHLEFRSIRGNLNTRLRKLDEQQEFSAIILATA GLQRMGWHNRVGQILHPEECMYAVGQGALGVEVRAKDQDI LDLVGVLHDPETLLRCIAERAFLRHLEGGCSVPVAVHTAM KDGQLYLTGGVWSLDGSDSIQETMQATIHVPAQHEDGPED DPQLVGITARNIPRGPQLAAQNLGISLANLLLSKGAKNIL DV Description Functional site 1) chain B residue 126 type sequence H description binding site for residue PO4 A 403 source : AC3 2) chain B residue 128 type sequence K description binding site for residue PO4 A 403 source : AC3 3) chain B residue 181 type sequence Q description binding site for residue PO4 A 403 source : AC3 4) chain B residue 26 type sequence R description binding site for residue PO4 B 402 source : AC5 5) chain B residue 34 type sequence Q description binding site for residue PO4 B 402 source : AC5 6) chain B residue 95 type sequence H description binding site for residue PO4 B 402 source : AC5 7) chain B residue 96 type sequence S description binding site for residue PO4 B 402 source : AC5 8) chain B residue 99 type sequence D description binding site for residue PO4 B 402 source : AC5 9) chain B residue 96 type sequence S description binding site for Di-peptide 7J8 B 401 and CYS B 261 source : AC6 10) chain B residue 98 type sequence K description binding site for Di-peptide 7J8 B 401 and CYS B 261 source : AC6 11) chain B residue 99 type sequence D description binding site for Di-peptide 7J8 B 401 and CYS B 261 source : AC6 12) chain B residue 100 type sequence L description binding site for Di-peptide 7J8 B 401 and CYS B 261 source : AC6 13) chain B residue 101 type sequence P description binding site for Di-peptide 7J8 B 401 and CYS B 261 source : AC6 14) chain B residue 102 type sequence T description binding site for Di-peptide 7J8 B 401 and CYS B 261 source : AC6 15) chain B residue 146 type sequence S description binding site for Di-peptide 7J8 B 401 and CYS B 261 source : AC6 16) chain B residue 147 type sequence S description binding site for Di-peptide 7J8 B 401 and CYS B 261 source : AC6 17) chain B residue 149 type sequence R description binding site for Di-peptide 7J8 B 401 and CYS B 261 source : AC6 18) chain B residue 150 type sequence R description binding site for Di-peptide 7J8 B 401 and CYS B 261 source : AC6 19) chain B residue 173 type sequence R description binding site for Di-peptide 7J8 B 401 and CYS B 261 source : AC6 20) chain B residue 189 type sequence A description binding site for Di-peptide 7J8 B 401 and CYS B 261 source : AC6 21) chain B residue 195 type sequence R description binding site for Di-peptide 7J8 B 401 and CYS B 261 source : AC6 22) chain B residue 214 type sequence A description binding site for Di-peptide 7J8 B 401 and CYS B 261 source : AC6 23) chain B residue 215 type sequence V description binding site for Di-peptide 7J8 B 401 and CYS B 261 source : AC6 24) chain B residue 217 type sequence Q description binding site for Di-peptide 7J8 B 401 and CYS B 261 source : AC6 25) chain B residue 218 type sequence G description binding site for Di-peptide 7J8 B 401 and CYS B 261 source : AC6 26) chain B residue 254 type sequence L description binding site for Di-peptide 7J8 B 401 and CYS B 261 source : AC6 27) chain B residue 259 type sequence G description binding site for Di-peptide 7J8 B 401 and CYS B 261 source : AC6 28) chain B residue 260 type sequence G description binding site for Di-peptide 7J8 B 401 and CYS B 261 source : AC6 29) chain B residue 262 type sequence S description binding site for Di-peptide 7J8 B 401 and CYS B 261 source : AC6 30) chain B residue 147 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI2 31) chain B residue 261 type MOD_RES sequence C description S-(dipyrrolylmethanemethyl)cysteine => ECO:0000269|PubMed:18936296 source Swiss-Prot : SWS_FT_FI4

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