eF-site ID 2i78-B PDB Code 2i78 Chain B click to enlarge Title Crystal structure of human dipeptidyl peptidase IV (DPP IV) complexed with ABT-341, a cyclohexene-constrained phenethylamine inhibitor Classification HYDROLASE Compound Dipeptidyl peptidase IV Source Homo sapiens (Human) (DPP4_HUMAN) Sequence B:  SRKTYTLTDYLKNTYRLKLYSLRWISDHEYLYKQENNILV FNAEYGNSSVFLENSTFDEFGHSINDYSISPDGQFILLEY NYVKQWRHSYTASYDIYDLNKRQLITEERIPNNTQWVTWS PVGHKLAYVWNNDIYVKIEPNLPSYRITWTGKEDIIYNGI TDWVYEEEVFSAYSALWWSPNGTFLAYAQFNDTEVPLIEY SFYSDESLQYPKTVRVPYPKAGAVNPTVKFFVVNTDSLSS VTNATSIQITAPASMLIGDHYLCDVTWATQERISLQWLRR IQNYSVMDICDYDESSGRWNCLVARQHIEMSTTGWVGRFR PSEPHFTLDGNSFYKIISNEEGYRHICYFQIDKKDCTFIT KGTWEVIGIEALTSDYLYYISNEYKGMPGGRNLYKIQLSD YTKVTCLSCELNPERCQYYSVSFSKEAKYYQLRCSGPGLP LYTLHSSVNDKGLRVLEDNSALDKMLQNVQMPSKKLDFII LNETKFWYQMILPPHFDKSKKYPLLLDVYAGPCSQKADTV FRLNWATYLASTENIIVASFDGRGSGYQGDKIMHAINRRL GTFEVEDQIEAARQFSKMGFVDNKRIAIWGWSYGGYVTSM VLGSGSGVFKCGIAVAPVSRWEYYDSVYTERYMGLPTPED NLDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQSAQ ISKALVDVGVDFQAMWYTDEDHGIASSTAHQHIYTHMSHF IKQCFS Description (1)  Dipeptidyl peptidase 4 (EC 3.4.14.5) (Dipeptidyl peptidase IV) (DPP IV) (T-cell activation antigen CD26) (TP103) (Adenosine deaminase complexing protein 2) (ADABP) Functional site 1) chain B residue 125 type sequence R description BINDING SITE FOR RESIDUE KIQ B 901 source : AC1 2) chain B residue 205 type sequence E description BINDING SITE FOR RESIDUE KIQ B 901 source : AC1 3) chain B residue 206 type sequence E description BINDING SITE FOR RESIDUE KIQ B 901 source : AC1 4) chain B residue 357 type sequence F description BINDING SITE FOR RESIDUE KIQ B 901 source : AC1 5) chain B residue 585 type sequence Y description BINDING SITE FOR RESIDUE KIQ B 901 source : AC1 6) chain B residue 630 type sequence S description BINDING SITE FOR RESIDUE KIQ B 901 source : AC1 7) chain B residue 631 type sequence Y description BINDING SITE FOR RESIDUE KIQ B 901 source : AC1 8) chain B residue 656 type sequence V description BINDING SITE FOR RESIDUE KIQ B 901 source : AC1 9) chain B residue 662 type sequence Y description BINDING SITE FOR RESIDUE KIQ B 901 source : AC1 10) chain B residue 666 type sequence Y description BINDING SITE FOR RESIDUE KIQ B 901 source : AC1 11) chain B residue 710 type sequence N description BINDING SITE FOR RESIDUE KIQ B 901 source : AC1 12) chain B residue 711 type sequence V description BINDING SITE FOR RESIDUE KIQ B 901 source : AC1 13) chain B residue 740 type sequence H description BINDING SITE FOR RESIDUE KIQ B 901 source : AC1 14) chain B residue 547 type catalytic sequence Y description 169 source MCSA : MCSA2 15) chain B residue 630 type catalytic sequence S description 169 source MCSA : MCSA2 16) chain B residue 631 type catalytic sequence Y description 169 source MCSA : MCSA2 17) chain B residue 708 type catalytic sequence D description 169 source MCSA : MCSA2 18) chain B residue 740 type catalytic sequence H description 169 source MCSA : MCSA2 19) chain B residue 630 type ACT_SITE sequence S description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084 source Swiss-Prot : SWS_FT_FI1 20) chain B residue 708 type ACT_SITE sequence D description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084 source Swiss-Prot : SWS_FT_FI1 21) chain B residue 740 type ACT_SITE sequence H description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084 source Swiss-Prot : SWS_FT_FI1 22) 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 23) 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 24) 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 25) 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 26) 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 27) 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 28) 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 29) 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 30) 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

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