eF-site ID 4cdf-ABCDEF PDB Code 4cdf Chain A, B, C, D, E, F click to enlarge Title Human DPP1 in complex with (2S,4S)-N-((1S)-1-cyano-2-(4-(4- cyanophenyl)phenyl)ethyl)-4-hydroxy-piperidine-2-carboxamide Classification HYDROLASE Compound DIPEPTIDYL PEPTIDASE 1 EXCLUSION DOMAIN CHAIN Source (CATC_HUMAN) Sequence A:  DTPANCTYLDLLGTWVFQVGSSGSQRDVNCSVMGPQEKKV VVYLQKLDTAYDDLGNSGHFTIIYNQGFEIVLNDYKWFAF FKYKEEGSKVTTYCNETMTGWVHDVLGRNWACFTGKKVGT B:  HLPTSWDWRNVHGINFVSPVRNQASCGSCYSFASMGMLEA RIRILTNNSQTPILSPQEVVSCSQYAQGCEGGFPYLIAGK YAQDFGLVEEACFPYTGTDSPCKMKEDCFRYYSSEYHYVG GFYGGCNEALMKLELVHHGPMAVAFEVYDDFLHYKKGIYH HT C:  PFNPFELTNHAVLLVGYGTDSASGMDYWIVKNSWGTGWGE NGYFRIRRGTDECAIESIAVAATPIPKL D:  DTPANCTYLDLLGTWVFQVGSSGSQRDVNCSVMGPQEKKV VVYLQKLDTAYDDLGNSGHFTIIYNQGFEIVLNDYKWFAF FKYKEEGSKVTTYCNETMTGWVHDVLGRNWACFTGKKV E:  LHLPTSWDWRNVHGINFVSPVRNQASCGSCYSFASMGMLE ARIRILTNNSQTPILSPQEVVSCSQYAQGCEGGFPYLIAG KYAQDFGLVEEACFPYTGTDSPCKMKEDCFRYYSSEYHYV GGFYGGCNEALMKLELVHHGPMAVAFEVYDDFLHYKKGIY HHT F:  PFNPFELTNHAVLLVGYGTDSASGMDYWIVKNSWGTGWGE NGYFRIRRGTDECAIESIAVAATPIPKL Description Functional site 1) chain C residue 379-389 type prosite sequence TNHAVLLVGYG description THIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. TNHAVLLVGYG source prosite : PS00639 2) chain C residue 398-417 type prosite sequence YWIVKNSWGTGWGENGYFRI description THIOL_PROTEASE_ASN Eukaryotic thiol (cysteine) proteases asparagine active site. YWIvKNSWgtgWGenGYFrI source prosite : PS00640 3) chain B residue 228-239 type prosite sequence QASCGSCYSFAS description THIOL_PROTEASE_CYS Eukaryotic thiol (cysteine) proteases cysteine active site. QAsCGSCYSfAS source prosite : PS00139 4) chain C residue 381 type ACT_SITE sequence H description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10089 source Swiss-Prot : SWS_FT_FI1 5) chain F residue 381 type ACT_SITE sequence H description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10089 source Swiss-Prot : SWS_FT_FI1 6) chain B residue 323 type ACT_SITE sequence Y description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10090 source Swiss-Prot : SWS_FT_FI2 7) chain E residue 278 type ACT_SITE sequence F description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10090 source Swiss-Prot : SWS_FT_FI2 8) chain C residue 403 type ACT_SITE sequence N description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10090 source Swiss-Prot : SWS_FT_FI2 9) chain F residue 403 type ACT_SITE sequence N description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10090 source Swiss-Prot : SWS_FT_FI2 10) chain E residue 280 type ACT_SITE sequence Y description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10090 source Swiss-Prot : SWS_FT_FI2 11) chain E residue 323 type ACT_SITE sequence Y description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10090 source Swiss-Prot : SWS_FT_FI2 12) chain B residue 252 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19167329 source Swiss-Prot : SWS_FT_FI3 13) chain E residue 252 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19167329 source Swiss-Prot : SWS_FT_FI3

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