eF-site ID 3edy-A PDB Code 3edy Chain A click to enlarge Title Crystal Structure of the Precursor Form of Human Tripeptidyl-Peptidase 1 Classification HYDROLASE Compound Tripeptidyl-peptidase 1 Source Homo sapiens (Human) (TPP1_HUMAN) Sequence A:  SYSPEPDQRRTLPPGWVSLGRADPEEELSLTFALRQQNVE RLSELVQAVSDPSSPQYGKYLTLENVADLVRPSPLTLHTV QKWLLAAGAQKCHSVITQDFLTCWLSIRQAELLLPGAEFH HYVGGPTETHVVRSPHPYQLPQALAPHVDFVGGLHRFPPT SSLRQRPEPQVTGTVGLHLGVTPSVIRKRYNLTSQDVGSG TSNNSQACAQFLEQYFHDSDLAQFMRLFGGNFAHQASVAR VVGQQGRGRAGIEASLDVQYLMSAGANISTWVYSSPGRHE GQEPFLQWLMLLSNESALPHVHTVSYGDDEDSLSSAYIQR VNTELMKAAARGLTLLFASGDSGAGCWSVSGRHQFRPTFP ASSPYVTTVGGTSFQEPFLITNEIVDYISGGGFSNVFPRP SYQEEAVTKFLSSSPHLPPSSYFNASGRAYPDVAALSDGY WVVSNRVPIPWVSGTSASTPVFGGILSLINEHRILSGRPP LGFLNPRLYQQHGAGLFDVTRGCHESCLDEEVEGQGFCSG PGWDPVTGWGTPNFPALLKTLLNP Description (1)  Crystal Structure of the Precursor Form of Human Tripeptidyl-Peptidase 1 Functional site 1) chain A residue 272 type ACT_SITE sequence E description Charge relay system => ECO:0000269|PubMed:19038966, ECO:0000269|PubMed:19038967 source Swiss-Prot : SWS_FT_FI1 2) chain A residue 276 type ACT_SITE sequence D description Charge relay system => ECO:0000269|PubMed:19038966, ECO:0000269|PubMed:19038967 source Swiss-Prot : SWS_FT_FI1 3) chain A residue 475 type ACT_SITE sequence S description Charge relay system => ECO:0000269|PubMed:19038966, ECO:0000269|PubMed:19038967, ECO:0000305|PubMed:11054422 source Swiss-Prot : SWS_FT_FI2 4) chain A residue 517 type BINDING sequence D description BINDING => ECO:0000269|PubMed:19038966, ECO:0000269|PubMed:19038967 source Swiss-Prot : SWS_FT_FI3 5) chain A residue 518 type BINDING sequence V description BINDING => ECO:0000269|PubMed:19038966, ECO:0000269|PubMed:19038967 source Swiss-Prot : SWS_FT_FI3 6) chain A residue 539 type BINDING sequence G description BINDING => ECO:0000269|PubMed:19038966, ECO:0000269|PubMed:19038967 source Swiss-Prot : SWS_FT_FI3 7) chain A residue 541 type BINDING sequence G description BINDING => ECO:0000269|PubMed:19038966, ECO:0000269|PubMed:19038967 source Swiss-Prot : SWS_FT_FI3 8) chain A residue 543 type BINDING sequence D description BINDING => ECO:0000269|PubMed:19038966, ECO:0000269|PubMed:19038967 source Swiss-Prot : SWS_FT_FI3 9) chain A residue 210 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19038966, ECO:0000269|PubMed:19038967, ECO:0000269|PubMed:19159218 source Swiss-Prot : SWS_FT_FI4 10) chain A residue 313 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19038966, ECO:0000269|PubMed:19038967, ECO:0000269|PubMed:19159218 source Swiss-Prot : SWS_FT_FI4 11) chain A residue 222 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 source Swiss-Prot : SWS_FT_FI5 12) chain A residue 286 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19038966, ECO:0000269|PubMed:19038967 source Swiss-Prot : SWS_FT_FI6 13) chain A residue 443 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:19038966, ECO:0000269|PubMed:19038967, ECO:0000269|PubMed:19159218 source Swiss-Prot : SWS_FT_FI7

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