eF-site ID 1nb5-ABCDIJKLPRST PDB Code 1nb5 Chain A, B, C, D, I, J, K, L, P, R, S, T click to enlarge Title Crystal structure of stefin A in complex with cathepsin H Classification HYDROLASE/HYDROLASE INHIBITOR Compound Cathepsin H Source ORGANISM_COMMON: pig; ORGANISM_SCIENTIFIC: Sus scrofa; Sequence A:  YPPSMDWRKKGNFVSPVKNQGSCGSCWTFSTTGALESAVA IATGKMLSLAEQQLVDCAQNFNNHGCQGGLPSQAFEYIRY NKGIMGEDTYPYKGQDDHCKFQPDKAIAFVKDVANITMND EEAMVEAVALYNPVSFAFEVTNDFLMYRKGIYSSTSCHKT PDKVNHAVLAVGYGEENGIPYWIVKNSWGPQWGMNGYFLI ERGKNMCGLAACASYPIPLV B:  YPPSMDWRKKGNFVSPVKNQGSCGSCWTFSTTGALESAVA IATGKMLSLAEQQLVDCAQNFNNHGCQGGLPSQAFEYIRY NKGIMGEDTYPYKGQDDHCKFQPDKAIAFVKDVANITMND EEAMVEAVALYNPVSFAFEVTNDFLMYRKGIYSSTSCHKT PDKVNHAVLAVGYGEENGIPYWIVKNSWGPQWGMNGYFLI ERGKNMCGLAACASYPIPLV C:  YPPSMDWRKKGNFVSPVKNQGSCGSCWTFSTTGALESAVA IATGKMLSLAEQQLVDCAQNFNNHGCQGGLPSQAFEYIRY NKGIMGEDTYPYKGQDDHCKFQPDKAIAFVKDVANITMND EEAMVEAVALYNPVSFAFEVTNDFLMYRKGIYSSTSCHKT PDKVNHAVLAVGYGEENGIPYWIVKNSWGPQWGMNGYFLI ERGKNMCGLAACASYPIPLV D:  YPPSMDWRKKGNFVSPVKNQGSCGSCWTFSTTGALESAVA IATGKMLSLAEQQLVDCAQNFNNHGCQGGLPSQAFEYIRY NKGIMGEDTYPYKGQDDHCKFQPDKAIAFVKDVANITMND EEAMVEAVALYNPVSFAFEVTNDFLMYRKGIYSSTSCHKT PDKVNHAVLAVGYGEENGIPYWIVKNSWGPQWGMNGYFLI ERGKNMCGLAACASYPIPLV I:  MIPGGLSEAKPATPEIQEIVDKVKPQLEEKTNETYGKLEA VQYKTQVVAGTNYYIKVRAGDNKYMHLKVFKSLPGQNEDL VLTGYQVDKNKDDELTGF J:  MIPGGLSEAKPATPEIQEIVDKVKPQLEEKTNETYGKLEA VQYKTQVVAGTNYYIKVRAGDNKYMHLKVFKSLPGQNEDL VLTGYQVDKNKDDELTGF K:  MIPGGLSEAKPATPEIQEIVDKVKPQLEEKTNETYGKLEA VQYKTQVVAGTNYYIKVRAGDNKYMHLKVFKSLPGQNEDL VLTGYQVDKNKDDELTGF L:  MIPGGLSEAKPATPEIQEIVDKVKPQLEEKTNETYGKLEA VQYKTQVVAGTNYYIKVRAGDNKYMHLKVFKSLPGQNEDL VLTGYQVDKNKDDELTGF P:  EPQNCSAT R:  EPQNCSAT S:  EPQNCSAT T:  EPQNCSAT Description Functional site 1) chain A residue 19 type catalytic sequence Q description 682 source MCSA : MCSA1 2) chain A residue 25 type catalytic sequence C description 682 source MCSA : MCSA1 3) chain A residue 159 type catalytic sequence H description 682 source MCSA : MCSA1 4) chain B residue 19 type catalytic sequence Q description 682 source MCSA : MCSA2 5) chain B residue 25 type catalytic sequence C description 682 source MCSA : MCSA2 6) chain B residue 159 type catalytic sequence H description 682 source MCSA : MCSA2 7) chain C residue 19 type catalytic sequence Q description 682 source MCSA : MCSA3 8) chain C residue 25 type catalytic sequence C description 682 source MCSA : MCSA3 9) chain C residue 159 type catalytic sequence H description 682 source MCSA : MCSA3 10) chain D residue 19 type catalytic sequence Q description 682 source MCSA : MCSA4 11) chain D residue 25 type catalytic sequence C description 682 source MCSA : MCSA4 12) chain D residue 159 type catalytic sequence H description 682 source MCSA : MCSA4 13) chain I residue 9 type SITE sequence G description Reactive site source Swiss-Prot : SWS_FT_FI1 14) chain D residue 25 type SITE sequence C description Reactive site source Swiss-Prot : SWS_FT_FI1 15) chain D residue 159 type SITE sequence H description Reactive site source Swiss-Prot : SWS_FT_FI1 16) chain D residue 175 type SITE sequence N description Reactive site source Swiss-Prot : SWS_FT_FI1 17) chain J residue 9 type SITE sequence G description Reactive site source Swiss-Prot : SWS_FT_FI1 18) chain K residue 9 type SITE sequence G description Reactive site source Swiss-Prot : SWS_FT_FI1 19) chain L residue 9 type SITE sequence G description Reactive site source Swiss-Prot : SWS_FT_FI1 20) chain B residue 159 type SITE sequence H description Reactive site source Swiss-Prot : SWS_FT_FI1 21) chain B residue 175 type SITE sequence N description Reactive site source Swiss-Prot : SWS_FT_FI1 22) chain C residue 25 type SITE sequence C description Reactive site source Swiss-Prot : SWS_FT_FI1 23) chain C residue 159 type SITE sequence H description Reactive site source Swiss-Prot : SWS_FT_FI1 24) chain C residue 175 type SITE sequence N description Reactive site source Swiss-Prot : SWS_FT_FI1 25) chain I residue 6 type MOD_RES sequence M description N-acetylmethionine => ECO:0000250|UniProtKB:P01039 source Swiss-Prot : SWS_FT_FI2 26) chain J residue 6 type MOD_RES sequence M description N-acetylmethionine => ECO:0000250|UniProtKB:P01039 source Swiss-Prot : SWS_FT_FI2 27) chain K residue 6 type MOD_RES sequence M description N-acetylmethionine => ECO:0000250|UniProtKB:P01039 source Swiss-Prot : SWS_FT_FI2 28) chain L residue 6 type MOD_RES sequence M description N-acetylmethionine => ECO:0000250|UniProtKB:P01039 source Swiss-Prot : SWS_FT_FI2 29) chain A residue 19-30 type prosite sequence QGSCGSCWTFST description THIOL_PROTEASE_CYS Eukaryotic thiol (cysteine) proteases cysteine active site. QGsCGSCWTfST source prosite : PS00139 30) chain A residue 157-167 type prosite sequence VNHAVLAVGYG description THIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. VNHAVLAVGYG source prosite : PS00639 31) chain A residue 170-189 type prosite sequence YWIVKNSWGPQWGMNGYFLI description THIOL_PROTEASE_ASN Eukaryotic thiol (cysteine) proteases asparagine active site. YWIvKNSWgpqWGmnGYFlI source prosite : PS00640 32) chain I residue 52-65 type prosite sequence TQVVAGTNYYIKVR description CYSTATIN Cysteine proteases inhibitors signature. TQVVAGTNYyIKVR source prosite : PS00287

Display surface Download Links