eF-site ID 1pad-A PDB Code 1pad Chain A click to enlarge Title Binding of chloromethyl ketone substrate analogues to crystalline papain Classification HYDROLASE/HYDROLASE INHIBITOR Compound PAPAIN Source Carica papaya (Papaya) (1PAD) Sequence A:  IPEYVDWRQKGAVTPVKNQGSCGSCWAFSAVVTIEGIIKI RTGNLNQYSEQELLDCDRRSYGCNGGYPWSALQLVAQYGI HYRNTYPYEGVQRYCRSREKGPYAAKTDGVRQVQPYNQGA LLYSIANQPVSVVLQAAGKDFQLYRGGIFVGPCGNKVDHA VAAVGYGPNYILIKNSWGTGWGENGYIRIKRGTGNSYGVC GLYTSSFYPVKN Description Functional site 1) chain A residue 11 type sequence G description BINDING SITE FOR CHAIN I OF ACETYL-ALA-ALA-PHE-ALA-CHLOROMETHYLKETONE INHIBITOR source : AC1 2) chain A residue 12 type sequence A description BINDING SITE FOR CHAIN I OF ACETYL-ALA-ALA-PHE-ALA-CHLOROMETHYLKETONE INHIBITOR source : AC1 3) chain A residue 14 type sequence T description BINDING SITE FOR CHAIN I OF ACETYL-ALA-ALA-PHE-ALA-CHLOROMETHYLKETONE INHIBITOR source : AC1 4) chain A residue 19 type sequence Q description BINDING SITE FOR CHAIN I OF ACETYL-ALA-ALA-PHE-ALA-CHLOROMETHYLKETONE INHIBITOR source : AC1 5) chain A residue 23 type sequence G description BINDING SITE FOR CHAIN I OF ACETYL-ALA-ALA-PHE-ALA-CHLOROMETHYLKETONE INHIBITOR source : AC1 6) chain A residue 24 type sequence S description BINDING SITE FOR CHAIN I OF ACETYL-ALA-ALA-PHE-ALA-CHLOROMETHYLKETONE INHIBITOR source : AC1 7) chain A residue 25 type sequence C description BINDING SITE FOR CHAIN I OF ACETYL-ALA-ALA-PHE-ALA-CHLOROMETHYLKETONE INHIBITOR source : AC1 8) chain A residue 35 type sequence E description BINDING SITE FOR CHAIN I OF ACETYL-ALA-ALA-PHE-ALA-CHLOROMETHYLKETONE INHIBITOR source : AC1 9) chain A residue 36 type sequence G description BINDING SITE FOR CHAIN I OF ACETYL-ALA-ALA-PHE-ALA-CHLOROMETHYLKETONE INHIBITOR source : AC1 10) chain A residue 39 type sequence K description BINDING SITE FOR CHAIN I OF ACETYL-ALA-ALA-PHE-ALA-CHLOROMETHYLKETONE INHIBITOR source : AC1 11) chain A residue 44 type sequence N description BINDING SITE FOR CHAIN I OF ACETYL-ALA-ALA-PHE-ALA-CHLOROMETHYLKETONE INHIBITOR source : AC1 12) chain A residue 45 type sequence L description BINDING SITE FOR CHAIN I OF ACETYL-ALA-ALA-PHE-ALA-CHLOROMETHYLKETONE INHIBITOR source : AC1 13) chain A residue 46 type sequence N description BINDING SITE FOR CHAIN I OF ACETYL-ALA-ALA-PHE-ALA-CHLOROMETHYLKETONE INHIBITOR source : AC1 14) chain A residue 47 type sequence Q description BINDING SITE FOR CHAIN I OF ACETYL-ALA-ALA-PHE-ALA-CHLOROMETHYLKETONE INHIBITOR source : AC1 15) chain A residue 48 type sequence Y description BINDING SITE FOR CHAIN I OF ACETYL-ALA-ALA-PHE-ALA-CHLOROMETHYLKETONE INHIBITOR source : AC1 16) chain A residue 61 type sequence Y description BINDING SITE FOR CHAIN I OF ACETYL-ALA-ALA-PHE-ALA-CHLOROMETHYLKETONE INHIBITOR source : AC1 17) chain A residue 65 type sequence G description BINDING SITE FOR CHAIN I OF ACETYL-ALA-ALA-PHE-ALA-CHLOROMETHYLKETONE INHIBITOR source : AC1 18) chain A residue 66 type sequence G description BINDING SITE FOR CHAIN I OF ACETYL-ALA-ALA-PHE-ALA-CHLOROMETHYLKETONE INHIBITOR source : AC1 19) chain A residue 67 type sequence Y description BINDING SITE FOR CHAIN I OF ACETYL-ALA-ALA-PHE-ALA-CHLOROMETHYLKETONE INHIBITOR source : AC1 20) chain A residue 133 type sequence V description BINDING SITE FOR CHAIN I OF ACETYL-ALA-ALA-PHE-ALA-CHLOROMETHYLKETONE INHIBITOR source : AC1 21) chain A residue 157 type sequence V description BINDING SITE FOR CHAIN I OF ACETYL-ALA-ALA-PHE-ALA-CHLOROMETHYLKETONE INHIBITOR source : AC1 22) chain A residue 158 type sequence D description BINDING SITE FOR CHAIN I OF ACETYL-ALA-ALA-PHE-ALA-CHLOROMETHYLKETONE INHIBITOR source : AC1 23) chain A residue 159 type sequence H description BINDING SITE FOR CHAIN I OF ACETYL-ALA-ALA-PHE-ALA-CHLOROMETHYLKETONE INHIBITOR source : AC1 24) chain A residue 19 type catalytic sequence Q description 174 source MCSA : MCSA1 25) chain A residue 25 type catalytic sequence C description 174 source MCSA : MCSA1 26) chain A residue 159 type catalytic sequence H description 174 source MCSA : MCSA1 27) chain A residue 175 type catalytic sequence N description 174 source MCSA : MCSA1 28) chain A residue 175 type ACT_SITE sequence N description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10090, ECO:0000269|PubMed:5681232, ECO:0000269|PubMed:6502713, ECO:0000269|PubMed:952885, ECO:0007744|PDB:1PAD, ECO:0007744|PDB:9PAP source Swiss-Prot : SWS_FT_FI3 29) chain A residue 25 type BINDING sequence C description covalent => ECO:0000269|PubMed:8416808, ECO:0007744|PDB:1POP source Swiss-Prot : SWS_FT_FI4 30) chain A residue 25 type ACT_SITE sequence C description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10088, ECO:0000269|PubMed:5681232, ECO:0000269|PubMed:6502713, ECO:0000269|PubMed:952885, ECO:0000305|PubMed:1860874, ECO:0007744|PDB:1PAD, ECO:0007744|PDB:9PAP source Swiss-Prot : SWS_FT_FI1 31) chain A residue 159 type ACT_SITE sequence H description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10089, ECO:0000269|PubMed:6502713, ECO:0000269|PubMed:952885, ECO:0007744|PDB:1PAD, ECO:0007744|PDB:9PAP source Swiss-Prot : SWS_FT_FI2 32) chain A residue 19-30 type prosite sequence QGSCGSCWAFSA description THIOL_PROTEASE_CYS Eukaryotic thiol (cysteine) proteases cysteine active site. QGsCGSCWAfSA source prosite : PS00139 33) chain A residue 157-167 type prosite sequence VDHAVAAVGYG description THIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. VDHAVAAVGYG source prosite : PS00639 34) chain A residue 170-189 type prosite sequence YILIKNSWGTGWGENGYIRI description THIOL_PROTEASE_ASN Eukaryotic thiol (cysteine) proteases asparagine active site. YILiKNSWgtgWGenGYIrI source prosite : PS00640

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