eF-site ID 2g5p-A PDB Code 2g5p Chain A click to enlarge Title Crystal structure of human dipeptidyl peptidase IV (DPPIV) complexed with cyanopyrrolidine (C5-pro-pro) inhibitor 21ac Classification HYDROLASE Compound Dipeptidyl peptidase 4 Source Homo sapiens (Human) (DPP4_HUMAN) Sequence A:  SRKTYTLTDYLKNTYRLKLYSLRWISDHEYLYKQENNILV FNAEYGNSSVFLENSTFDEFGHSINDYSISPDGQFILLEY NYVKQWRHSYTASYDIYDLNKRQLITEERIPNNTQWVTWS PVGHKLAYVWNNDIYVKIEPNLPSYRITWTGKEDIIYNGI TDWVYEEEVFSAYSALWWSPNGTFLAYAQFNDTEVPLIEY SFYSDESLQYPKTVRVPYPKAGAVNPTVKFFVVNTDSLSS VTNATSIQITAPASMLIGDHYLCDVTWATQERISLQWLRR IQNYSVMDICDYDESSGRWNCLVARQHIEMSTTGWVGRFR PSEPHFTLDGNSFYKIISNEEGYRHICYFQIDKKDCTFIT KGTWEVIGIEALTSDYLYYISNEYKGMPGGRNLYKIQLSD YTKVTCLSCELNPERCQYYSVSFSKEAKYYQLRCSGPGLP LYTLHSSVNDKGLRVLEDNSALDKMLQNVQMPSKKLDFII LNETKFWYQMILPPHFDKSKKYPLLLDVYAGPCSQKADTV FRLNWATYLASTENIIVASFDGRGSGYQGDKIMHAINRRL GTFEVEDQIEAARQFSKMGFVDNKRIAIWGWSYGGYVTSM VLGSGSGVFKCGIAVAPVSRWEYYDSVYTERYMGLPTPED NLDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQSAQ ISKALVDVGVDFQAMWYTDEDHGIASSTAHQHIYTHMSHF IKQCFS Description (1)  Dipeptidyl peptidase 4 Functional site 1) chain A residue 205 type sequence E description BINDING SITE FOR RESIDUE ADF A 800 source : AC1 2) chain A residue 206 type sequence E description BINDING SITE FOR RESIDUE ADF A 800 source : AC1 3) chain A residue 209 type sequence S description BINDING SITE FOR RESIDUE ADF A 800 source : AC1 4) chain A residue 547 type sequence Y description BINDING SITE FOR RESIDUE ADF A 800 source : AC1 5) chain A residue 630 type sequence S description BINDING SITE FOR RESIDUE ADF A 800 source : AC1 6) chain A residue 631 type sequence Y description BINDING SITE FOR RESIDUE ADF A 800 source : AC1 7) chain A residue 656 type sequence V description BINDING SITE FOR RESIDUE ADF A 800 source : AC1 8) chain A residue 662 type sequence Y description BINDING SITE FOR RESIDUE ADF A 800 source : AC1 9) chain A residue 666 type sequence Y description BINDING SITE FOR RESIDUE ADF A 800 source : AC1 10) chain A residue 710 type sequence N description BINDING SITE FOR RESIDUE ADF A 800 source : AC1 11) chain A residue 547 type catalytic sequence Y description 169 source MCSA : MCSA1 12) chain A residue 630 type catalytic sequence S description 169 source MCSA : MCSA1 13) chain A residue 631 type catalytic sequence Y description 169 source MCSA : MCSA1 14) chain A residue 708 type catalytic sequence D description 169 source MCSA : MCSA1 15) chain A residue 740 type catalytic sequence H description 169 source MCSA : MCSA1 16) chain A residue 630 type ACT_SITE sequence S description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084 source Swiss-Prot : SWS_FT_FI1 17) chain A residue 708 type ACT_SITE sequence D description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084 source Swiss-Prot : SWS_FT_FI1 18) chain A residue 740 type ACT_SITE sequence H description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084 source Swiss-Prot : SWS_FT_FI1 19) 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 20) 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 21) 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 22) 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 23) 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 24) 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 25) 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 26) 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 27) 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 28) chain A residue 605-635 type prosite sequence DQIEAARQFSKMGFVDNKRIAIWGWSYGGYV description PRO_ENDOPEP_SER Prolyl endopeptidase family serine active site. DqieAarqFskmgfvdnkriaiwGwSyGGYV source prosite : PS00708

Display surface Download Links