eF-site ID 1aqn-A PDB Code 1aqn Chain A click to enlarge Title SUBTILISIN MUTANT 8324 Classification SERINE PROTEASE Compound SUBTILISIN 8324 Source Bacillus amyloliquefaciens (Bacillus velezensis) (SUBT_BACAM) Sequence A:  AQSVPYGVSQIKAPALHSQGYCGSNVKVAVIDSGIDSSHP DLKVAGGASFVPSETNPFQDNNSHGTHVAGTVAALNNSIG VLGVAPCASLYAVKVLGADGSGQYSWIINGIEWAIANNMD VINMSLGGPSGSAALKAAVDKAVASGVVVVAAAGNEGTSG SSSTVGYPAKYPSVIAVGAVDSSNQRASFSSVGPELDVMA PGVSICSTLPGNKYGAKSGTSMASPHVAGAAALILSKHPN WTNTQVRSSLENTTTKLGDSFYYGKGLINVQAAAQ Description Functional site 1) chain A residue 22 type sequence C description MUTATION FROM THR TO CYS AT RESIDUE 22. CYS 22 FORMS A DISULFIDE BOND WITH CYS 87. source : C22 2) chain A residue 50 type sequence F description MUTATION FROM MET TO PHE AT RESIDUE 50. source : F50 3) chain A residue 87 type sequence C description MUTATION FROM SER TO CYS AT RESIDUE 87. CYS 87 FORMS A DISULFIDE BOND WITH CYS 22. source : C87 4) chain A residue 169 type sequence A description MUTATION FROM GLY TO ALA AT RESIDUE 169. source : 169 5) chain A residue 206 type sequence C description MUTATION FROM GLN TO CYS AT RESIDUE 206. SOME UNKNOWN COMPOUND IS BOUND TO THE SG. source : 206 6) chain A residue 217 type sequence K description MUTATION FROM TYR TO LYS AT RESIDUE 217. source : 217 7) chain A residue 218 type sequence S description MUTATION FROM ASN TO SER AT RESIDUE 218. source : 218 8) chain A residue 2 type sequence Q description BINDING SITE FOR RESIDUE CA A 295 source : AC1 9) chain A residue 41 type sequence D description BINDING SITE FOR RESIDUE CA A 295 source : AC1 10) chain A residue 75 type sequence L description BINDING SITE FOR RESIDUE CA A 295 source : AC1 11) chain A residue 77 type sequence N description BINDING SITE FOR RESIDUE CA A 295 source : AC1 12) chain A residue 79 type sequence I description BINDING SITE FOR RESIDUE CA A 295 source : AC1 13) chain A residue 81 type sequence V description BINDING SITE FOR RESIDUE CA A 295 source : AC1 14) chain A residue 195 type sequence E description BINDING SITE FOR RESIDUE CA A 297 source : AC2 15) chain A residue 197 type sequence D description BINDING SITE FOR RESIDUE CA A 297 source : AC2 16) chain A residue 206 type sequence C description BINDING SITE FOR RESIDUE UNX A 277 source : AC3 17) chain A residue 206 type sequence C description BINDING SITE FOR RESIDUE UNX A 278 source : AC4 18) chain A residue 215 type sequence G description BINDING SITE FOR RESIDUE UNX A 278 source : AC4 19) chain A residue 58 type sequence F description BINDING SITE FOR RESIDUE IPA A 290 source : AC5 20) chain A residue 186 type sequence R description BINDING SITE FOR RESIDUE IPA A 290 source : AC5 21) chain A residue 145 type sequence S description BINDING SITE FOR RESIDUE IPA A 291 source : AC6 22) chain A residue 189 type sequence F description BINDING SITE FOR RESIDUE IPA A 291 source : AC6 23) chain A residue 2 type BINDING sequence Q description source Swiss-Prot : SWS_FT_FI2 24) chain A residue 41 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 25) chain A residue 75 type BINDING sequence L description source Swiss-Prot : SWS_FT_FI2 26) chain A residue 77 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2 27) chain A residue 79 type BINDING sequence I description source Swiss-Prot : SWS_FT_FI2 28) chain A residue 81 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI2 29) chain A residue 169 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI2 30) chain A residue 171 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI2 31) chain A residue 174 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI2 32) chain A residue 32 type ACT_SITE sequence D description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240, ECO:0000269|PubMed:5249818 source Swiss-Prot : SWS_FT_FI1 33) chain A residue 64 type ACT_SITE sequence H description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240, ECO:0000269|PubMed:5249818 source Swiss-Prot : SWS_FT_FI1 34) chain A residue 221 type ACT_SITE sequence S description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240, ECO:0000269|PubMed:5249818 source Swiss-Prot : SWS_FT_FI1 35) chain A residue 32 type catalytic sequence D description 723 source MCSA : MCSA1 36) chain A residue 64 type catalytic sequence H description 723 source MCSA : MCSA1 37) chain A residue 155 type catalytic sequence N description 723 source MCSA : MCSA1 38) chain A residue 221 type catalytic sequence S description 723 source MCSA : MCSA1 39) chain A residue 28-39 type prosite sequence VAVIDSGIDSSH description SUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. VAVIDSGIdssH source prosite : PS00136 40) chain A residue 64-74 type prosite sequence HGTHVAGTVAA description SUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGThVAGtVAA source prosite : PS00137 41) chain A residue 219-229 type prosite sequence GTSMASPHVAG description SUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSmAsPhVAG source prosite : PS00138

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