eF-site ID 4yct-A PDB Code 4yct Chain A click to enlarge Title Endothiapepsin in complex with fragment 216 Classification HYDROLASE Compound Endothiapepsin Source ORGANISM_COMMON: Chesnut blight fungus; ORGANISM_SCIENTIFIC: Cryphonectria parasitica; Sequence A:  STGSATTTPIDSLDDAYITPVQIGTPAQTLNLDFDTGSSD LWVFSSETTASEVDGQTIYTPSKSTTAKLLSGATWSISYG SSSSGDVYTDTVSVGGLTVTGQAVESAKKVSSSFTEDSTI DGLLGLAFSTLNTVSPTQQKTFFDNAKASLDSPVFTADLG YHAPGTYNFGFIDTTAYTGSITYTAVSTKQGFWEWTSTGY AVGSGTFKSTSIDGIADTGTTLLYLPATVVSAYWAQVSGA KSSSSVGGYVFPCSATLPSFTFGVGSARIVIPGDYIDFGP ISTGSSSCFGGIQSSAGIGINIFGDVALKAAFVVFNGATT PTLGFASK Description Functional site 1) chain A residue 35 type sequence D description binding site for residue FBF A 401 source : AC1 2) chain A residue 37 type sequence G description binding site for residue FBF A 401 source : AC1 3) chain A residue 38 type sequence S description binding site for residue FBF A 401 source : AC1 4) chain A residue 79 type sequence Y description binding site for residue FBF A 401 source : AC1 5) chain A residue 219 type sequence D description binding site for residue FBF A 401 source : AC1 6) chain A residue 300 type sequence I description binding site for residue FBF A 401 source : AC1 7) chain A residue 302 type sequence I description binding site for residue FBF A 401 source : AC1 8) chain A residue 272 type sequence V description binding site for residue GOL A 402 source : AC2 9) chain A residue 277 type sequence Y description binding site for residue GOL A 402 source : AC2 10) chain A residue 312 type sequence A description binding site for residue GOL A 402 source : AC2 11) chain A residue 329 type sequence S description binding site for residue GOL A 402 source : AC2 12) chain A residue 330 type sequence K description binding site for residue GOL A 402 source : AC2 13) chain A residue 187 type sequence A description binding site for residue EDO A 403 source : AC3 14) chain A residue 198 type sequence T description binding site for residue EDO A 403 source : AC3 15) chain A residue 215 type sequence D description binding site for residue EDO A 403 source : AC3 16) chain A residue 255 type sequence C description binding site for residue ACT A 404 source : AC4 17) chain A residue 279 type sequence D description binding site for residue ACT A 404 source : AC4 18) chain A residue 281 type sequence G description binding site for residue ACT A 404 source : AC4 19) chain A residue 290 type sequence C description binding site for residue ACT A 404 source : AC4 20) chain A residue 15 type sequence D description binding site for residue PEG A 405 source : AC5 21) chain A residue 223 type sequence T description binding site for residue PEG A 405 source : AC5 22) chain A residue 224 type sequence L description binding site for residue PEG A 405 source : AC5 23) chain A residue 280 type sequence F description binding site for residue PEG A 405 source : AC5 24) chain A residue 297 type sequence S description binding site for residue GOL A 406 source : AC6 25) chain A residue 301 type sequence G description binding site for residue GOL A 406 source : AC6 26) chain A residue 302 type sequence I description binding site for residue GOL A 406 source : AC6 27) chain A residue 32-43 type prosite sequence LDFDTGSSDLWV description ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. LDFDTGSSDLWV source prosite : PS00141 28) chain A residue 216-227 type prosite sequence GIADTGTTLLYL description ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. LDFDTGSSDLWV source prosite : PS00141 29) chain A residue 35 type ACT_SITE sequence D description source Swiss-Prot : SWS_FT_FI1 30) chain A residue 199 type ACT_SITE sequence S description source Swiss-Prot : SWS_FT_FI1

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