eF-site ID 1z8g-A PDB Code 1z8g Chain A click to enlarge Title Crystal structure of the extracellular region of the transmembrane serine protease hepsin with covalently bound preferred substrate. Classification HYDROLASE/HYDROLASE INHIBITOR Compound Serine protease hepsin Source Homo sapiens (Human) (1Z8G) Sequence A:  EPLYPVQVSSADARLMVFDKTEGTWRLLCSSRSNARVAGL SCEEMGFLRALTHSELDVRTAGAAGTSGFFCVDEGRLPHT QRLLEVISVCDCPRGRFLAAICQDCGRRKLPIVGGRDTSL GRWPWQVSLRYDGAHLCGGSLLSGDWVLTAAHCFPERNRV LSRWRVFAGAVAQASPHGLQLGVQAVVYHGGYLPFRDPNS EENSNDIALVHLSSPLPLTEYIQPVCLPAAGQALVDGKIC TVTGWGNTQYYGQQAGVLQEARVPIISNDVCNGADFYGNQ IKPKMFCAGYPEGGIDACQGDSGGPFVCEDSISRTPRWRL CGIVSWGTGCALAQKPGVYTKVSDFREWIFQAIKTHSEAS GMVTQL Description Functional site 1) chain A residue 203 type sequence H description BINDING SITE FOR CHAIN L OF ACE-LYS-GLN-LEU-ARG-CHLOROMETHYLKETONE source : AC1 2) chain A residue 243 type sequence Y description BINDING SITE FOR CHAIN L OF ACE-LYS-GLN-LEU-ARG-CHLOROMETHYLKETONE source : AC1 3) chain A residue 252 type sequence E description BINDING SITE FOR CHAIN L OF ACE-LYS-GLN-LEU-ARG-CHLOROMETHYLKETONE source : AC1 4) chain A residue 254 type sequence N description BINDING SITE FOR CHAIN L OF ACE-LYS-GLN-LEU-ARG-CHLOROMETHYLKETONE source : AC1 5) chain A residue 301 type sequence Y description BINDING SITE FOR CHAIN L OF ACE-LYS-GLN-LEU-ARG-CHLOROMETHYLKETONE source : AC1 6) chain A residue 331 type sequence Q description BINDING SITE FOR CHAIN L OF ACE-LYS-GLN-LEU-ARG-CHLOROMETHYLKETONE source : AC1 7) chain A residue 347 type sequence D description BINDING SITE FOR CHAIN L OF ACE-LYS-GLN-LEU-ARG-CHLOROMETHYLKETONE source : AC1 8) chain A residue 348 type sequence A description BINDING SITE FOR CHAIN L OF ACE-LYS-GLN-LEU-ARG-CHLOROMETHYLKETONE source : AC1 9) chain A residue 349 type sequence C description BINDING SITE FOR CHAIN L OF ACE-LYS-GLN-LEU-ARG-CHLOROMETHYLKETONE source : AC1 10) chain A residue 350 type sequence Q description BINDING SITE FOR CHAIN L OF ACE-LYS-GLN-LEU-ARG-CHLOROMETHYLKETONE source : AC1 11) chain A residue 351 type sequence G description BINDING SITE FOR CHAIN L OF ACE-LYS-GLN-LEU-ARG-CHLOROMETHYLKETONE source : AC1 12) chain A residue 353 type sequence S description BINDING SITE FOR CHAIN L OF ACE-LYS-GLN-LEU-ARG-CHLOROMETHYLKETONE source : AC1 13) chain A residue 376 type sequence S description BINDING SITE FOR CHAIN L OF ACE-LYS-GLN-LEU-ARG-CHLOROMETHYLKETONE source : AC1 14) chain A residue 377 type sequence W description BINDING SITE FOR CHAIN L OF ACE-LYS-GLN-LEU-ARG-CHLOROMETHYLKETONE source : AC1 15) chain A residue 378 type sequence G description BINDING SITE FOR CHAIN L OF ACE-LYS-GLN-LEU-ARG-CHLOROMETHYLKETONE source : AC1 16) chain A residue 379 type sequence T description BINDING SITE FOR CHAIN L OF ACE-LYS-GLN-LEU-ARG-CHLOROMETHYLKETONE source : AC1 17) chain A residue 380 type sequence G description BINDING SITE FOR CHAIN L OF ACE-LYS-GLN-LEU-ARG-CHLOROMETHYLKETONE source : AC1 18) chain A residue 381 type sequence C description BINDING SITE FOR CHAIN L OF ACE-LYS-GLN-LEU-ARG-CHLOROMETHYLKETONE source : AC1 19) chain A residue 388 type sequence G description BINDING SITE FOR CHAIN L OF ACE-LYS-GLN-LEU-ARG-CHLOROMETHYLKETONE source : AC1 20) chain A residue 203 type ACT_SITE sequence H description Charge relay system => ECO:0000305|PubMed:12962630, ECO:0000305|PubMed:15839837 source Swiss-Prot : SWS_FT_FI1 21) chain A residue 257 type ACT_SITE sequence D description Charge relay system => ECO:0000305|PubMed:12962630, ECO:0000305|PubMed:15839837 source Swiss-Prot : SWS_FT_FI1 22) chain A residue 353 type ACT_SITE sequence S description Charge relay system => ECO:0000305|PubMed:12962630, ECO:0000305|PubMed:15839837 source Swiss-Prot : SWS_FT_FI1 23) chain A residue 112 type CARBOHYD sequence A description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 source Swiss-Prot : SWS_FT_FI2 24) chain A residue 199-204 type prosite sequence LTAAHC description TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC source prosite : PS00134 25) chain A residue 347-358 type prosite sequence DACQGDSGGPFV description TRYPSIN_SER Serine proteases, trypsin family, serine active site. DAcqGDSGGPFV source prosite : PS00135

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