eF-site ID 4pv7-AB PDB Code 4pv7 Chain A, B click to enlarge Title Cocrystal structure of dipeptidyl-peptidase 4 with an indole scaffold inhibitor Classification HYDROLASE/HYDROLASE INHIBITOR Compound Dipeptidyl peptidase 4 soluble form Source Homo sapiens (Human) (DPP4_HUMAN) Sequence A:  RKTYTLTDYLKNTYRLKLYSLRWISDHEYLYKQENNILVF NAEYGNSSVFLENSTFDEFGHSINDYSISPDGQFILLEYN YVKQWRHSYTASYDIYDLNKRQLITEERIPNNTQWVTWSP VGHKLAYVWNNDIYVKIEPNLPSYRITWTGKEDIIYNGIT DWVYEEEVFSAYSALWWSPNGTFLAYAQFNDTEVPLIEYS FYSDESLQYPKTVRVPYPKAGAVNPTVKFFVVNTDSLSSV TNATSIQITAPASMLIGDHYLCDVTWATQERISLQWLRRI QNYSVMDICDYDESSGRWNCLVARQHIEMSTTGWVGRFRP SEPHFTLDGNSFYKIISNEEGYRHICYFQIDKKDCTFITK GTWEVIGIEALTSDYLYYISNEYKGMPGGRNLYKIQLSDY TKVTCLSCELNPERCQYYSVSFSKEAKYYQLRCSGPGLPL YTLHSSVNDKGLRVLEDNSALDKMLQNVQMPSKKLDFIIL NETKFWYQMILPPHFDKSKKYPLLLDVYAGPCSQKADTVF RLNWATYLASTENIIVASFDGRGSGYQGDKIMHAINRRLG TFEVEDQIEAARQFSKMGFVDNKRIAIWGWSYGGYVTSMV LGSGSGVFKCGIAVAPVSRWEYYDSVYTERYMGLPTPEDN LDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQSAQI SKALVDVGVDFQAMWYTDEDHGIASSTAHQHIYTHMSHFI KQCFSLP B:  RKTYTLTDYLKNTYRLKLYSLRWISDHEYLYKQENNILVF NAEYGNSSVFLENSTFDEFGHSINDYSISPDGQFILLEYN YVKQWRHSYTASYDIYDLNKRQLITEERIPNNTQWVTWSP VGHKLAYVWNNDIYVKIEPNLPSYRITWTGKEDIIYNGIT DWVYEEEVFSAYSALWWSPNGTFLAYAQFNDTEVPLIEYS FYSDESLQYPKTVRVPYPKAGAVNPTVKFFVVNTDSLSSV TNATSIQITAPASMLIGDHYLCDVTWATQERISLQWLRRI QNYSVMDICDYDESSGRWNCLVARQHIEMSTTGWVGRFRP SEPHFTLDGNSFYKIISNEEGYRHICYFQIDKKDCTFITK GTWEVIGIEALTSDYLYYISNEYKGMPGGRNLYKIQLSDY TKVTCLSCELNPERCQYYSVSFSKEAKYYQLRCSGPGLPL YTLHSSVNDKGLRVLEDNSALDKMLQNVQMPSKKLDFIIL NETKFWYQMILPPHFDKSKKYPLLLDVYAGPCSQKADTVF RLNWATYLASTENIIVASFDGRGSGYQGDKIMHAINRRLG TFEVEDQIEAARQFSKMGFVDNKRIAIWGWSYGGYVTSMV LGSGSGVFKCGIAVAPVSRWEYYDSVYTERYMGLPTPEDN LDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQSAQI SKALVDVGVDFQAMWYTDEDHGIASSTAHQHIYTHMSHFI KQCFSLP Description (1)  Dipeptidyl peptidase 4 soluble form (E.C.3.4.14.5) Functional site 1) chain A residue 125 type sequence R description BINDING SITE FOR RESIDUE CJP A 1000 source : AC1 2) chain A residue 205 type sequence E description BINDING SITE FOR RESIDUE CJP A 1000 source : AC1 3) chain A residue 206 type sequence E description BINDING SITE FOR RESIDUE CJP A 1000 source : AC1 4) chain A residue 547 type sequence Y description BINDING SITE FOR RESIDUE CJP A 1000 source : AC1 5) chain A residue 630 type sequence S description BINDING SITE FOR RESIDUE CJP A 1000 source : AC1 6) chain A residue 656 type sequence V description BINDING SITE FOR RESIDUE CJP A 1000 source : AC1 7) chain A residue 662 type sequence Y description BINDING SITE FOR RESIDUE CJP A 1000 source : AC1 8) chain A residue 666 type sequence Y description BINDING SITE FOR RESIDUE CJP A 1000 source : AC1 9) chain A residue 710 type sequence N description BINDING SITE FOR RESIDUE CJP A 1000 source : AC1 10) chain A residue 740 type sequence H description BINDING SITE FOR RESIDUE CJP A 1000 source : AC1 11) chain B residue 125 type sequence R description BINDING SITE FOR RESIDUE CJP B 1000 source : AC2 12) chain B residue 205 type sequence E description BINDING SITE FOR RESIDUE CJP B 1000 source : AC2 13) chain B residue 206 type sequence E description BINDING SITE FOR RESIDUE CJP B 1000 source : AC2 14) chain B residue 547 type sequence Y description BINDING SITE FOR RESIDUE CJP B 1000 source : AC2 15) chain B residue 630 type sequence S description BINDING SITE FOR RESIDUE CJP B 1000 source : AC2 16) chain B residue 656 type sequence V description BINDING SITE FOR RESIDUE CJP B 1000 source : AC2 17) chain B residue 662 type sequence Y description BINDING SITE FOR RESIDUE CJP B 1000 source : AC2 18) chain B residue 666 type sequence Y description BINDING SITE FOR RESIDUE CJP B 1000 source : AC2 19) chain B residue 740 type sequence H description BINDING SITE FOR RESIDUE CJP B 1000 source : AC2 20) chain A residue 547 type catalytic sequence Y description 169 source MCSA : MCSA1 21) chain A residue 630 type catalytic sequence S description 169 source MCSA : MCSA1 22) chain A residue 631 type catalytic sequence Y description 169 source MCSA : MCSA1 23) chain A residue 708 type catalytic sequence D description 169 source MCSA : MCSA1 24) chain A residue 740 type catalytic sequence H description 169 source MCSA : MCSA1 25) chain B residue 547 type catalytic sequence Y description 169 source MCSA : MCSA2 26) chain B residue 630 type catalytic sequence S description 169 source MCSA : MCSA2 27) chain B residue 631 type catalytic sequence Y description 169 source MCSA : MCSA2 28) chain B residue 708 type catalytic sequence D description 169 source MCSA : MCSA2 29) chain B residue 740 type catalytic sequence H description 169 source MCSA : MCSA2 30) chain A residue 92 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72 source Swiss-Prot : SWS_FT_FI3 31) chain B residue 92 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72 source Swiss-Prot : SWS_FT_FI3 32) chain A residue 150 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72 source Swiss-Prot : SWS_FT_FI4 33) chain B residue 150 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72 source Swiss-Prot : SWS_FT_FI4 34) chain A residue 219 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72 source Swiss-Prot : SWS_FT_FI5 35) chain B residue 219 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72 source Swiss-Prot : SWS_FT_FI5 36) chain A residue 281 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72 source Swiss-Prot : SWS_FT_FI6 37) chain B residue 281 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72 source Swiss-Prot : SWS_FT_FI6 38) chain A residue 321 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72 source Swiss-Prot : SWS_FT_FI7 39) chain B residue 321 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72 source Swiss-Prot : SWS_FT_FI7 40) chain A residue 520 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72 source Swiss-Prot : SWS_FT_FI8 41) chain B residue 520 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72 source Swiss-Prot : SWS_FT_FI8 42) chain A residue 685 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218 source Swiss-Prot : SWS_FT_FI9 43) chain B residue 685 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218 source Swiss-Prot : SWS_FT_FI9 44) chain A residue 630 type ACT_SITE sequence S description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084 source Swiss-Prot : SWS_FT_FI1 45) chain A residue 708 type ACT_SITE sequence D description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084 source Swiss-Prot : SWS_FT_FI1 46) chain A residue 740 type ACT_SITE sequence H description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084 source Swiss-Prot : SWS_FT_FI1 47) chain B residue 630 type ACT_SITE sequence S description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084 source Swiss-Prot : SWS_FT_FI1 48) chain B residue 708 type ACT_SITE sequence D description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084 source Swiss-Prot : SWS_FT_FI1 49) chain B residue 740 type ACT_SITE sequence H description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084 source Swiss-Prot : SWS_FT_FI1 50) chain A residue 85 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72 source Swiss-Prot : SWS_FT_FI2 51) chain A residue 229 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72 source Swiss-Prot : SWS_FT_FI2 52) chain B residue 85 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72 source Swiss-Prot : SWS_FT_FI2 53) chain B residue 229 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72 source Swiss-Prot : SWS_FT_FI2 54) chain A residue 605-635 type prosite sequence DQIEAARQFSKMGFVDNKRIAIWGWSYGGYV description PRO_ENDOPEP_SER Prolyl endopeptidase family serine active site. DqieAarqFskmgfvdnkriaiwGwSyGGYV source prosite : PS00708

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