eF-site ID 1psa-A PDB Code 1psa Chain A click to enlarge Title STRUCTURE OF A PEPSIN(SLASH)RENIN INHIBITOR COMPLEX REVEALS A NOVEL CRYSTAL PACKING INDUCED BY MINOR CHEMICAL ALTERATIONS IN THE INHIBITOR Classification HYDROLASE/hydrolase inhibitor Compound PEPSIN A Source Sus scrofa (Pig) (PEPA_PIG) Sequence A:  IGDEPLENYLDTEYFGTIGIGTPAQDFTVIFDTGSSNLWV PSVYCSSLACSDHNQFNPDDSSTFEATSQELSITYGTGSM TGILGYDTVQVGGISDTNQIFGLSETEPGSFLYYAPFDGI LGLAYPSISASGATPVFDNLWDQGLVSQDLFSVYLSSNDD SGSVVLLGGIDSSYYTGSLNWVPVSVEGYWQITLDSITMD GETIACSGGCQAIVDTGTSLLTGPTSAIANIQSDIGASEN SDGEMVISCSSIDSLPDIVFTINGVQYPLSPSAYILQDDD SCTSGFEGMDVPTSSGELWILGDVFIRQYYTVFDRANNKV GLAPVA Description (1)  PEPSIN HYDROLASE (ACID PROTEINASE) (E.C.3.4.23.1) COMPLEX WITH A-62095 Functional site 1) chain A residue 32 type sequence D description BINDING SITE FOR RESIDUE 0ZL A 327 source : AC1 2) chain A residue 34 type sequence G description BINDING SITE FOR RESIDUE 0ZL A 327 source : AC1 3) chain A residue 75 type sequence Y description BINDING SITE FOR RESIDUE 0ZL A 327 source : AC1 4) chain A residue 76 type sequence G description BINDING SITE FOR RESIDUE 0ZL A 327 source : AC1 5) chain A residue 77 type sequence T description BINDING SITE FOR RESIDUE 0ZL A 327 source : AC1 6) chain A residue 120 type sequence I description BINDING SITE FOR RESIDUE 0ZL A 327 source : AC1 7) chain A residue 213 type sequence I description BINDING SITE FOR RESIDUE 0ZL A 327 source : AC1 8) chain A residue 215 type sequence D description BINDING SITE FOR RESIDUE 0ZL A 327 source : AC1 9) chain A residue 217 type sequence G description BINDING SITE FOR RESIDUE 0ZL A 327 source : AC1 10) chain A residue 218 type sequence T description BINDING SITE FOR RESIDUE 0ZL A 327 source : AC1 11) chain A residue 219 type sequence S description BINDING SITE FOR RESIDUE 0ZL A 327 source : AC1 12) chain A residue 289 type sequence M description BINDING SITE FOR RESIDUE 0ZL A 327 source : AC1 13) chain A residue 300 type sequence I description BINDING SITE FOR RESIDUE 0ZL A 327 source : AC1 14) chain A residue 29-40 type prosite sequence VIFDTGSSNLWV description ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. VIFDTGSSNLWV source prosite : PS00141 15) chain A residue 212-223 type prosite sequence AIVDTGTSLLTG description ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. VIFDTGSSNLWV source prosite : PS00141 16) chain A residue 32 type ACT_SITE sequence D description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094, ECO:0000269|PubMed:1097438, ECO:0000269|PubMed:4897201 source Swiss-Prot : SWS_FT_FI1 17) chain A residue 215 type ACT_SITE sequence D description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094, ECO:0000269|PubMed:1097438, ECO:0000269|PubMed:4897201 source Swiss-Prot : SWS_FT_FI1 18) chain A residue 68 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P03954 source Swiss-Prot : SWS_FT_FI2

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