eF-site ID 1czi-EP PDB Code 1czi Chain E, P click to enlarge Title CHYMOSIN COMPLEX WITH THE INHIBITOR CP-113972 Classification HYDROLASE/HYDROLASE INHIBITOR Compound CHYMOSIN Source Bos taurus (Bovine) (1CZI) Sequence E:  GEVASVPLTNYLDSQYFGKIYLGTPPQEFTVLFDTGSSDF WVPSIYCKSNACKNHQRFDPRKSSTFQNLGKPLSIHYGTG SMQGILGYDTVTVSNIVDIQQTVGLSTQEPGDVFTYAEFD GILGMAYPSLASEYSIPVFDNMMNRHLVAQDLFSVYMDRN GQESMLTLGAIDPSYYTGSLHWVPVTVQQYWQFTVDSVTI SGVVVACEGGCQAILDTGTSKLVGPSSDILNIQQAIGATQ NQYGEFDIDCDNLSYMPTVVFEINGKMYPLTPSAYTSQDQ GFCTSGFQSENHSQKWILGDVFIREYYSVFDRANNLVGLA KAI P:  PXXX Description Functional site 1) chain E residue 32 type sequence D description ACTIVE SITE. source : AC1 2) chain E residue 215 type sequence D description ACTIVE SITE. source : AC2 3) chain E residue 12 type sequence S description BINDING SITE FOR CHAIN P OF CP-113972 (NORSTATINE-S-METHYL CYSTEINE-IODO-PHENYLALANINE- source : AC3 4) chain E residue 13 type sequence Q description BINDING SITE FOR CHAIN P OF CP-113972 (NORSTATINE-S-METHYL CYSTEINE-IODO-PHENYLALANINE- source : AC3 5) chain E residue 32 type sequence D description BINDING SITE FOR CHAIN P OF CP-113972 (NORSTATINE-S-METHYL CYSTEINE-IODO-PHENYLALANINE- source : AC3 6) chain E residue 34 type sequence G description BINDING SITE FOR CHAIN P OF CP-113972 (NORSTATINE-S-METHYL CYSTEINE-IODO-PHENYLALANINE- source : AC3 7) chain E residue 75 type sequence Y description BINDING SITE FOR CHAIN P OF CP-113972 (NORSTATINE-S-METHYL CYSTEINE-IODO-PHENYLALANINE- source : AC3 8) chain E residue 76 type sequence G description BINDING SITE FOR CHAIN P OF CP-113972 (NORSTATINE-S-METHYL CYSTEINE-IODO-PHENYLALANINE- source : AC3 9) chain E residue 77 type sequence T description BINDING SITE FOR CHAIN P OF CP-113972 (NORSTATINE-S-METHYL CYSTEINE-IODO-PHENYLALANINE- source : AC3 10) chain E residue 111 type sequence V description BINDING SITE FOR CHAIN P OF CP-113972 (NORSTATINE-S-METHYL CYSTEINE-IODO-PHENYLALANINE- source : AC3 11) chain E residue 112 type sequence F description BINDING SITE FOR CHAIN P OF CP-113972 (NORSTATINE-S-METHYL CYSTEINE-IODO-PHENYLALANINE- source : AC3 12) chain E residue 117 type sequence F description BINDING SITE FOR CHAIN P OF CP-113972 (NORSTATINE-S-METHYL CYSTEINE-IODO-PHENYLALANINE- source : AC3 13) chain E residue 120 type sequence I description BINDING SITE FOR CHAIN P OF CP-113972 (NORSTATINE-S-METHYL CYSTEINE-IODO-PHENYLALANINE- source : AC3 14) chain E residue 213 type sequence I description BINDING SITE FOR CHAIN P OF CP-113972 (NORSTATINE-S-METHYL CYSTEINE-IODO-PHENYLALANINE- source : AC3 15) chain E residue 215 type sequence D description BINDING SITE FOR CHAIN P OF CP-113972 (NORSTATINE-S-METHYL CYSTEINE-IODO-PHENYLALANINE- source : AC3 16) chain E residue 217 type sequence G description BINDING SITE FOR CHAIN P OF CP-113972 (NORSTATINE-S-METHYL CYSTEINE-IODO-PHENYLALANINE- source : AC3 17) chain E residue 218 type sequence T description BINDING SITE FOR CHAIN P OF CP-113972 (NORSTATINE-S-METHYL CYSTEINE-IODO-PHENYLALANINE- source : AC3 18) chain E residue 219 type sequence S description BINDING SITE FOR CHAIN P OF CP-113972 (NORSTATINE-S-METHYL CYSTEINE-IODO-PHENYLALANINE- source : AC3 19) chain E residue 220 type sequence K description BINDING SITE FOR CHAIN P OF CP-113972 (NORSTATINE-S-METHYL CYSTEINE-IODO-PHENYLALANINE- source : AC3 20) chain E residue 287 type sequence Q description BINDING SITE FOR CHAIN P OF CP-113972 (NORSTATINE-S-METHYL CYSTEINE-IODO-PHENYLALANINE- source : AC3 21) chain E residue 300 type sequence I description BINDING SITE FOR CHAIN P OF CP-113972 (NORSTATINE-S-METHYL CYSTEINE-IODO-PHENYLALANINE- source : AC3 22) chain E residue 29-40 type prosite sequence VLFDTGSSDFWV description ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. VLFDTGSSDFWV source prosite : PS00141 23) chain E residue 212-223 type prosite sequence AILDTGTSKLVG description ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. VLFDTGSSDFWV source prosite : PS00141 24) chain E residue 32 type ACT_SITE sequence D description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094, ECO:0000269|PubMed:329280, ECO:0000269|PubMed:4612029 source Swiss-Prot : SWS_FT_FI1 25) chain E residue 215 type ACT_SITE sequence D description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094, ECO:0000269|PubMed:329280, ECO:0000269|PubMed:4612029 source Swiss-Prot : SWS_FT_FI1

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