eF-site ID 1psa-AB PDB Code 1psa Chain A, B 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 B:  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 B residue 30 type sequence I description BINDING SITE FOR RESIDUE 0ZL B 327 source : AC2 15) chain B residue 32 type sequence D description BINDING SITE FOR RESIDUE 0ZL B 327 source : AC2 16) chain B residue 34 type sequence G description BINDING SITE FOR RESIDUE 0ZL B 327 source : AC2 17) chain B residue 75 type sequence Y description BINDING SITE FOR RESIDUE 0ZL B 327 source : AC2 18) chain B residue 76 type sequence G description BINDING SITE FOR RESIDUE 0ZL B 327 source : AC2 19) chain B residue 77 type sequence T description BINDING SITE FOR RESIDUE 0ZL B 327 source : AC2 20) chain B residue 111 type sequence F description BINDING SITE FOR RESIDUE 0ZL B 327 source : AC2 21) chain B residue 117 type sequence F description BINDING SITE FOR RESIDUE 0ZL B 327 source : AC2 22) chain B residue 189 type sequence Y description BINDING SITE FOR RESIDUE 0ZL B 327 source : AC2 23) chain B residue 213 type sequence I description BINDING SITE FOR RESIDUE 0ZL B 327 source : AC2 24) chain B residue 215 type sequence D description BINDING SITE FOR RESIDUE 0ZL B 327 source : AC2 25) chain B residue 217 type sequence G description BINDING SITE FOR RESIDUE 0ZL B 327 source : AC2 26) chain B residue 218 type sequence T description BINDING SITE FOR RESIDUE 0ZL B 327 source : AC2 27) chain B residue 219 type sequence S description BINDING SITE FOR RESIDUE 0ZL B 327 source : AC2 28) chain B residue 289 type sequence M description BINDING SITE FOR RESIDUE 0ZL B 327 source : AC2 29) chain A residue 29-40 type prosite sequence VIFDTGSSNLWV description ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. VIFDTGSSNLWV source prosite : PS00141 30) chain A residue 212-223 type prosite sequence AIVDTGTSLLTG description ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. VIFDTGSSNLWV source prosite : PS00141 31) 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 32) 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 33) chain B 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 34) chain B 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 35) chain A residue 68 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P03954 source Swiss-Prot : SWS_FT_FI2 36) chain B residue 68 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P03954 source Swiss-Prot : SWS_FT_FI2

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