eF-site ID 2g63-ABCD PDB Code 2g63 Chain A, B, C, D click to enlarge Title Crystal structure of human dipeptidyl peptidase IV (DPPIV) complexed with cyanopyrrolidine (C5-pro-pro) inhibitor 24b 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 B:  SRKTYTLTDYLKNTYRLKLYSLRWISDHEYLYKQENNILV FNAEYGNSSVFLENSTFDEFGHSINDYSISPDGQFILLEY NYVKQWRHSYTASYDIYDLNKRQLITEERIPNNTQWVTWS PVGHKLAYVWNNDIYVKIEPNLPSYRITWTGKEDIIYNGI TDWVYEEEVFSAYSALWWSPNGTFLAYAQFNDTEVPLIEY SFYSDESLQYPKTVRVPYPKAGAVNPTVKFFVVNTDSLSS VTNATSIQITAPASMLIGDHYLCDVTWATQERISLQWLRR IQNYSVMDICDYDESSGRWNCLVARQHIEMSTTGWVGRFR PSEPHFTLDGNSFYKIISNEEGYRHICYFQIDKKDCTFIT KGTWEVIGIEALTSDYLYYISNEYKGMPGGRNLYKIQLSD YTKVTCLSCELNPERCQYYSVSFSKEAKYYQLRCSGPGLP LYTLHSSVNDKGLRVLEDNSALDKMLQNVQMPSKKLDFII LNETKFWYQMILPPHFDKSKKYPLLLDVYAGPCSQKADTV FRLNWATYLASTENIIVASFDGRGSGYQGDKIMHAINRRL GTFEVEDQIEAARQFSKMGFVDNKRIAIWGWSYGGYVTSM VLGSGSGVFKCGIAVAPVSRWEYYDSVYTERYMGLPTPED NLDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQSAQ ISKALVDVGVDFQAMWYTDEDHGIASSTAHQHIYTHMSHF IKQCFS C:  SRKTYTLTDYLKNTYRLKLYSLRWISDHEYLYKQENNILV FNAEYGNSSVFLENSTFDEFGHSINDYSISPDGQFILLEY NYVKQWRHSYTASYDIYDLNKRQLITEERIPNNTQWVTWS PVGHKLAYVWNNDIYVKIEPNLPSYRITWTGKEDIIYNGI TDWVYEEEVFSAYSALWWSPNGTFLAYAQFNDTEVPLIEY SFYSDESLQYPKTVRVPYPKAGAVNPTVKFFVVNTDSLSS VTNATSIQITAPASMLIGDHYLCDVTWATQERISLQWLRR IQNYSVMDICDYDESSGRWNCLVARQHIEMSTTGWVGRFR PSEPHFTLDGNSFYKIISNEEGYRHICYFQIDKKDCTFIT KGTWEVIGIEALTSDYLYYISNEYKGMPGGRNLYKIQLSD YTKVTCLSCELNPERCQYYSVSFSKEAKYYQLRCSGPGLP LYTLHSSVNDKGLRVLEDNSALDKMLQNVQMPSKKLDFII LNETKFWYQMILPPHFDKSKKYPLLLDVYAGPCSQKADTV FRLNWATYLASTENIIVASFDGRGSGYQGDKIMHAINRRL GTFEVEDQIEAARQFSKMGFVDNKRIAIWGWSYGGYVTSM VLGSGSGVFKCGIAVAPVSRWEYYDSVYTERYMGLPTPED NLDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQSAQ ISKALVDVGVDFQAMWYTDEDHGIASSTAHQHIYTHMSHF IKQCFS D:  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 B residue 125 type sequence R description BINDING SITE FOR RESIDUE AAF B 800 source : AC1 2) chain B residue 205 type sequence E description BINDING SITE FOR RESIDUE AAF B 800 source : AC1 3) chain B residue 206 type sequence E description BINDING SITE FOR RESIDUE AAF B 800 source : AC1 4) chain B residue 547 type sequence Y description BINDING SITE FOR RESIDUE AAF B 800 source : AC1 5) chain B residue 553 type sequence Q description BINDING SITE FOR RESIDUE AAF B 800 source : AC1 6) chain B residue 630 type sequence S description BINDING SITE FOR RESIDUE AAF B 800 source : AC1 7) chain B residue 631 type sequence Y description BINDING SITE FOR RESIDUE AAF B 800 source : AC1 8) chain B residue 656 type sequence V description BINDING SITE FOR RESIDUE AAF B 800 source : AC1 9) chain B residue 662 type sequence Y description BINDING SITE FOR RESIDUE AAF B 800 source : AC1 10) chain B residue 666 type sequence Y description BINDING SITE FOR RESIDUE AAF B 800 source : AC1 11) chain B residue 710 type sequence N description BINDING SITE FOR RESIDUE AAF B 800 source : AC1 12) chain A residue 547 type catalytic sequence Y description 169 source MCSA : MCSA1 13) chain A residue 630 type catalytic sequence S description 169 source MCSA : MCSA1 14) chain A residue 631 type catalytic sequence Y description 169 source MCSA : MCSA1 15) chain A residue 708 type catalytic sequence D description 169 source MCSA : MCSA1 16) chain A residue 740 type catalytic sequence H description 169 source MCSA : MCSA1 17) chain B residue 547 type catalytic sequence Y description 169 source MCSA : MCSA2 18) chain B residue 630 type catalytic sequence S description 169 source MCSA : MCSA2 19) chain B residue 631 type catalytic sequence Y description 169 source MCSA : MCSA2 20) chain B residue 708 type catalytic sequence D description 169 source MCSA : MCSA2 21) chain B residue 740 type catalytic sequence H description 169 source MCSA : MCSA2 22) chain C residue 547 type catalytic sequence Y description 169 source MCSA : MCSA3 23) chain C residue 630 type catalytic sequence S description 169 source MCSA : MCSA3 24) chain C residue 631 type catalytic sequence Y description 169 source MCSA : MCSA3 25) chain C residue 708 type catalytic sequence D description 169 source MCSA : MCSA3 26) chain C residue 740 type catalytic sequence H description 169 source MCSA : MCSA3 27) chain D residue 547 type catalytic sequence Y description 169 source MCSA : MCSA4 28) chain D residue 630 type catalytic sequence S description 169 source MCSA : MCSA4 29) chain D residue 631 type catalytic sequence Y description 169 source MCSA : MCSA4 30) chain D residue 708 type catalytic sequence D description 169 source MCSA : MCSA4 31) chain D residue 740 type catalytic sequence H description 169 source MCSA : MCSA4 32) chain A residue 605-635 type prosite sequence DQIEAARQFSKMGFVDNKRIAIWGWSYGGYV description PRO_ENDOPEP_SER Prolyl endopeptidase family serine active site. DqieAarqFskmgfvdnkriaiwGwSyGGYV source prosite : PS00708 33) chain A residue 630 type ACT_SITE sequence S description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084 source Swiss-Prot : SWS_FT_FI1 34) chain D residue 630 type ACT_SITE sequence S description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084 source Swiss-Prot : SWS_FT_FI1 35) chain D residue 708 type ACT_SITE sequence D description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084 source Swiss-Prot : SWS_FT_FI1 36) chain D residue 740 type ACT_SITE sequence H description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084 source Swiss-Prot : SWS_FT_FI1 37) chain A residue 708 type ACT_SITE sequence D description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084 source Swiss-Prot : SWS_FT_FI1 38) chain A residue 740 type ACT_SITE sequence H description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084 source Swiss-Prot : SWS_FT_FI1 39) chain B residue 630 type ACT_SITE sequence S description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084 source Swiss-Prot : SWS_FT_FI1 40) chain B residue 708 type ACT_SITE sequence D description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084 source Swiss-Prot : SWS_FT_FI1 41) chain B residue 740 type ACT_SITE sequence H description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084 source Swiss-Prot : SWS_FT_FI1 42) chain C residue 630 type ACT_SITE sequence S description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084 source Swiss-Prot : SWS_FT_FI1 43) chain C residue 708 type ACT_SITE sequence D description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084 source Swiss-Prot : SWS_FT_FI1 44) chain C residue 740 type ACT_SITE sequence H description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084 source Swiss-Prot : SWS_FT_FI1 45) 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 46) 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 47) 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 48) 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 49) chain C 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 50) chain C 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 51) chain D 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 52) chain D 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 53) 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 54) 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 55) chain C 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 56) chain D 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 57) 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 58) 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 59) chain C 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 60) chain D 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 61) 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 62) 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 63) chain C 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 64) chain D 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 65) 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 66) 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 67) chain C 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 68) chain D 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 69) 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 70) 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 71) chain C 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 72) chain D 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 73) 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 74) 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 75) chain C 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 76) chain D 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 77) 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 78) 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 79) chain C 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 80) chain D 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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