eF-site ID 2gbf-AB PDB Code 2gbf Chain A, B click to enlarge Title rat dpp-IV with alkynyl cyanopyrrolidine #1 Classification HYDROLASE Compound Dipeptidyl peptidase 4 Source ORGANISM_COMMON: Norway rat; ORGANISM_SCIENTIFIC: Rattus norvegicus; Sequence A:  RRTYTLADYLKNTFRVKSYSLRWVSDSEYLYKQENNILLF NAEHGNSSIFLENSTFEIFGDSISDYSVSPDRLFVLLEYN YVKQWRHSYTASYSIYDLNKRQLITEEKIPNNTQWITWSQ EGHKLAYVWKNDIYVKIEPHLPSHRITSTGKENVIFNGIN DWVYEEEIFGAYSALWWSPNGTFLAYAQFNDTGVPLIEYS FYSDESLQYPKTVWIPYPKAGAVNPTVKFFIVNTDSLSST TTTIPMQITAPASVTTGDHYLCDVAWVSEDRISLQWLRRI QNYSVMAICDYDKTTLVWNCPTTQEHIETSATGWCGRFRP AEPHFTSDGSSFYKIVSDKDGYKHICQFQKDRKPEQVCTF ITKGAWEVISIEALTSDYLYYISNEYKEMPGGRNLYKIQL TDHTNKKCLSCDLNPERCQYYSVSLSKEAKYYQLGCRGPG LPLYTLHRSTDQKELRVLEDNSALDKMLQDVQMPSKKLDF IVLNETRFWYQMILPPHFDKSKKYPLLIDVYAGPCSQKAD AAFRLNWATYLASTENIIVASFDGRGSGYQGDKIMHAINK RLGTLEVEDQIEAARQFLKMGFVDSKRVAIWGWSYGGYVT SMVLGSGSGVFKCGIAVAPVSRWEYYDSVYTERYMGLPTP EDNLDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQS AQISKALVDAGVDFQAMWYTDEDHGIASSTAHQHIYSHMS HFLQQCFSLR B:  RRTYTLADYLKNTFRVKSYSLRWVSDSEYLYKQENNILLF NAEHGNSSIFLENSTFEIFGDSISDYSVSPDRLFVLLEYN YVKQWRHSYTASYSIYDLNKRQLITEEKIPNNTQWITWSQ EGHKLAYVWKNDIYVKIEPHLPSHRITSTGKENVIFNGIN DWVYEEEIFGAYSALWWSPNGTFLAYAQFNDTGVPLIEYS FYSDESLQYPKTVWIPYPKAGAVNPTVKFFIVNTDSLSST TTTIPMQITAPASVTTGDHYLCDVAWVSEDRISLQWLRRI QNYSVMAICDYDKTTLVWNCPTTQEHIETSATGWCGRFRP AEPHFTSDGSSFYKIVSDKDGYKHICQFQKDRKPEQVCTF ITKGAWEVISIEALTSDYLYYISNEYKEMPGGRNLYKIQL TDHTNKKCLSCDLNPERCQYYSVSLSKEAKYYQLGCRGPG LPLYTLHRSTDQKELRVLEDNSALDKMLQDVQMPSKKLDF IVLNETRFWYQMILPPHFDKSKKYPLLIDVYAGPCSQKAD AAFRLNWATYLASTENIIVASFDGRGSGYQGDKIMHAINK RLGTLEVEDQIEAARQFLKMGFVDSKRVAIWGWSYGGYVT SMVLGSGSGVFKCGIAVAPVSRWEYYDSVYTERYMGLPTP EDNLDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQS AQISKALVDAGVDFQAMWYTDEDHGIASSTAHQHIYSHMS HFLQQCFSLR Description (1)  Dipeptidyl peptidase 4 (EC 3.4.14.5) Functional site 1) chain A residue 123 type sequence R description BINDING SITE FOR RESIDUE AIA A 768 source : AC1 2) chain A residue 203 type sequence E description BINDING SITE FOR RESIDUE AIA A 768 source : AC1 3) chain A residue 204 type sequence E description BINDING SITE FOR RESIDUE AIA A 768 source : AC1 4) chain A residue 548 type sequence Y description BINDING SITE FOR RESIDUE AIA A 768 source : AC1 5) chain A residue 631 type sequence S description BINDING SITE FOR RESIDUE AIA A 768 source : AC1 6) chain A residue 632 type sequence Y description BINDING SITE FOR RESIDUE AIA A 768 source : AC1 7) chain A residue 663 type sequence Y description BINDING SITE FOR RESIDUE AIA A 768 source : AC1 8) chain A residue 667 type sequence Y description BINDING SITE FOR RESIDUE AIA A 768 source : AC1 9) chain A residue 711 type sequence N description BINDING SITE FOR RESIDUE AIA A 768 source : AC1 10) chain A residue 148 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 11) chain A residue 217 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 12) chain A residue 686 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 13) chain B residue 148 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 14) chain B residue 217 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 15) chain B residue 686 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 16) chain B residue 631 type ACT_SITE sequence S description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084 source Swiss-Prot : SWS_FT_FI1 17) chain B residue 709 type ACT_SITE sequence D description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084 source Swiss-Prot : SWS_FT_FI1 18) chain B residue 741 type ACT_SITE sequence H description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084 source Swiss-Prot : SWS_FT_FI1 19) chain A residue 631 type ACT_SITE sequence S description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084 source Swiss-Prot : SWS_FT_FI1 20) chain A residue 709 type ACT_SITE sequence D description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084 source Swiss-Prot : SWS_FT_FI1 21) chain A residue 741 type ACT_SITE sequence H description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084 source Swiss-Prot : SWS_FT_FI1 22) chain A residue 227 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16768443 source Swiss-Prot : SWS_FT_FI2 23) chain A residue 319 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16768443 source Swiss-Prot : SWS_FT_FI2 24) chain A residue 521 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16768443 source Swiss-Prot : SWS_FT_FI2 25) chain B residue 83 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16768443 source Swiss-Prot : SWS_FT_FI2 26) chain B residue 90 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16768443 source Swiss-Prot : SWS_FT_FI2 27) chain B residue 227 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16768443 source Swiss-Prot : SWS_FT_FI2 28) chain B residue 319 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16768443 source Swiss-Prot : SWS_FT_FI2 29) chain B residue 521 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16768443 source Swiss-Prot : SWS_FT_FI2 30) chain A residue 90 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16768443 source Swiss-Prot : SWS_FT_FI2 31) chain A residue 83 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16768443 source Swiss-Prot : SWS_FT_FI2 32) chain A residue 323-337 type prosite sequence MAICDYDKTTLVWNC description WD_REPEATS_1 Trp-Asp (WD) repeats signature. MAICdyDkTTLVWNC source prosite : PS00678 33) chain A residue 606-636 type prosite sequence DQIEAARQFLKMGFVDSKRVAIWGWSYGGYV description PRO_ENDOPEP_SER Prolyl endopeptidase family serine active site. DqieAarqFlkmgfvdskrvaiwGwSyGGYV source prosite : PS00708

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