eF-site ID 1itu-A PDB Code 1itu Chain A click to enlarge Title HUMAN RENAL DIPEPTIDASE COMPLEXED WITH CILASTATIN Classification HYDROLASE Compound RENAL DIPEPTIDASE Source (MDP1_HUMAN) Sequence A:  DFFRDEAERIMRDSPVIDGHNDLPWQLLDMFNNRLQDERA NLTTLAGTHTNIPKLRAGFVGGQFWSVYTPCDTQNKDAVR RTLEQMDVVHRMCRMYPETFLYVTSSAGIRQAFREGKVAS LIGVEGGHSIDSSLGVLRALYQLGMRYLTLTHSCNTPWAD NWLVDTGDSEPQSQGLSPFGQRVVKELNRLGVLIDLAHVS VATMKATLQLSRAPVIFSHSSAYSVCASRRNVPDDVLRLV KQTDSLVMVNFYNNYISCTNKANLSQVADHLDHIKEVAGA RAVGFGGDFDGVPRVPEGLEDVSKYPDLIAELLRRNWTEA EVKGALADNLLRVFEAVEQASNLTQAPEEEPIPLDQLGGS CRTHYGYSS Description Functional site 1) chain A residue 20 type catalytic sequence H description 168 source MCSA : MCSA1 2) chain A residue 22 type catalytic sequence D description 168 source MCSA : MCSA1 3) chain A residue 125 type catalytic sequence E description 168 source MCSA : MCSA1 4) chain A residue 152 type catalytic sequence H description 168 source MCSA : MCSA1 5) chain A residue 198 type catalytic sequence H description 168 source MCSA : MCSA1 6) chain A residue 219 type catalytic sequence H description 168 source MCSA : MCSA1 7) chain A residue 288 type catalytic sequence D description 168 source MCSA : MCSA1 8) chain A residue 263 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 source Swiss-Prot : SWS_FT_FI6 9) chain A residue 316 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12144777 source Swiss-Prot : SWS_FT_FI7 10) chain A residue 342 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI8 11) chain A residue 124-146 type prosite sequence VEGGHSIDSSLGVLRALYQLGMR description RENAL_DIPEPTIDASE_1 Renal dipeptidase active site. VEGGhsIdsslgvLralYqlGMR source prosite : PS00869 12) chain A residue 20 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU10073, ECO:0000269|PubMed:12144777 source Swiss-Prot : SWS_FT_FI1 13) chain A residue 22 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU10073, ECO:0000269|PubMed:12144777 source Swiss-Prot : SWS_FT_FI1 14) chain A residue 198 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU10073, ECO:0000269|PubMed:12144777 source Swiss-Prot : SWS_FT_FI1 15) chain A residue 219 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU10073, ECO:0000269|PubMed:12144777 source Swiss-Prot : SWS_FT_FI1 16) chain A residue 125 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU10073, ECO:0000269|PubMed:12144777, ECO:0000269|PubMed:32325220 source Swiss-Prot : SWS_FT_FI2 17) chain A residue 152 type BINDING sequence H description BINDING => ECO:0000269|PubMed:12144777 source Swiss-Prot : SWS_FT_FI3 18) chain A residue 230 type BINDING sequence R description BINDING => ECO:0000269|PubMed:12144777 source Swiss-Prot : SWS_FT_FI3 19) chain A residue 288 type BINDING sequence D description BINDING => ECO:0000269|PubMed:12144777 source Swiss-Prot : SWS_FT_FI3 20) chain A residue 369 type LIPID sequence S description GPI-anchor amidated serine => ECO:0000269|PubMed:2168407 source Swiss-Prot : SWS_FT_FI4 21) chain A residue 41 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12144777, ECO:0000269|PubMed:19159218 source Swiss-Prot : SWS_FT_FI5

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