eF-site ID 1sbc-A PDB Code 1sbc Chain A click to enlarge Title THE REFINED CRYSTAL STRUCTURE OF SUBTILISIN CARLSBERG AT 2.5 ANGSTROMS RESOLUTION Classification SERINE PROTEINASE Compound SUBTILISIN CARLSBERG Source Bacillus licheniformis (SUBT_BACLI) Sequence A:  AQTVPYGIPLIKADKVQAQGFKGANVKVAVLDTGIQASHP DLNVVGGASFVAGEAYNTDGNGHGTHVAGTVAALDNTTGV LGVAPSVSLYAVKVLNSSGSGSYSGIVSGIEWATTNGMDV INMSLGGASGSTAMKQAVDNAYARGVVVVAAAGNSGNSGS TNTIGYPAKYDSVIAVGAVDSNSNRASFSSVGAELEVMAP GAGVYSTYPTNTYATLNGTSMASPHVAGAAALILSKHPNL SASQVRNRLSSTATYLGSSFYYGKGLINVEAAAQ Description Functional site 1) chain A residue 32 type sequence D description RESIDUES OF THE CATALYTIC TRIAD source : CAT 2) chain A residue 64 type sequence H description RESIDUES OF THE CATALYTIC TRIAD source : CAT 3) chain A residue 221 type sequence S description RESIDUES OF THE CATALYTIC TRIAD source : CAT 4) chain A residue 125 type sequence S description THREE RESIDUES CAPABLE OF FORMING AN ANTIPARALLEL BETA-SHEET WITH SUBSTRATE OR INHIBITOR RESIDUES P1 - P3 source : S13 5) chain A residue 126 type sequence L description THREE RESIDUES CAPABLE OF FORMING AN ANTIPARALLEL BETA-SHEET WITH SUBSTRATE OR INHIBITOR RESIDUES P1 - P3 source : S13 6) chain A residue 127 type sequence G description THREE RESIDUES CAPABLE OF FORMING AN ANTIPARALLEL BETA-SHEET WITH SUBSTRATE OR INHIBITOR RESIDUES P1 - P3 source : S13 7) chain A residue 102 type sequence G description ADDITIONAL ACTIVE SITE LOOP CAPABLE OF HYDROGEN BONDING WITH RESIDUES P4 AND P6 OF SUBSTRATE source : S46 8) chain A residue 103 type sequence S description ADDITIONAL ACTIVE SITE LOOP CAPABLE OF HYDROGEN BONDING WITH RESIDUES P4 AND P6 OF SUBSTRATE source : S46 9) chain A residue 104 type sequence Y description ADDITIONAL ACTIVE SITE LOOP CAPABLE OF HYDROGEN BONDING WITH RESIDUES P4 AND P6 OF SUBSTRATE source : S46 10) chain A residue 2 type sequence Q description BINDING SITE FOR RESIDUE CA A 276 source : AC1 11) chain A residue 41 type sequence D description BINDING SITE FOR RESIDUE CA A 276 source : AC1 12) chain A residue 75 type sequence L description BINDING SITE FOR RESIDUE CA A 276 source : AC1 13) chain A residue 77 type sequence N description BINDING SITE FOR RESIDUE CA A 276 source : AC1 14) chain A residue 79 type sequence T description BINDING SITE FOR RESIDUE CA A 276 source : AC1 15) chain A residue 81 type sequence V description BINDING SITE FOR RESIDUE CA A 276 source : AC1 16) chain A residue 28-39 type prosite sequence VAVLDTGIQASH description SUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. VAVLDTGIqasH source prosite : PS00136 17) chain A residue 64-74 type prosite sequence HGTHVAGTVAA description SUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGThVAGtVAA source prosite : PS00137 18) chain A residue 219-229 type prosite sequence GTSMASPHVAG description SUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSmAsPhVAG source prosite : PS00138 19) chain A residue 32 type ACT_SITE sequence D description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240 source Swiss-Prot : SWS_FT_FI1 20) chain A residue 64 type ACT_SITE sequence H description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240 source Swiss-Prot : SWS_FT_FI1 21) chain A residue 221 type ACT_SITE sequence S description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240 source Swiss-Prot : SWS_FT_FI1 22) chain A residue 2 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:8512925 source Swiss-Prot : SWS_FT_FI2 23) chain A residue 41 type BINDING sequence D description BINDING => ECO:0000269|PubMed:8512925 source Swiss-Prot : SWS_FT_FI2 24) chain A residue 75 type BINDING sequence L description BINDING => ECO:0000269|PubMed:8512925 source Swiss-Prot : SWS_FT_FI2 25) chain A residue 77 type BINDING sequence N description BINDING => ECO:0000269|PubMed:8512925 source Swiss-Prot : SWS_FT_FI2 26) chain A residue 79 type BINDING sequence T description BINDING => ECO:0000269|PubMed:8512925 source Swiss-Prot : SWS_FT_FI2 27) chain A residue 81 type BINDING sequence V description BINDING => ECO:0000269|PubMed:8512925 source Swiss-Prot : SWS_FT_FI2 28) chain A residue 169 type BINDING sequence A description BINDING => ECO:0000269|PubMed:8512925 source Swiss-Prot : SWS_FT_FI2 29) chain A residue 171 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:8512925 source Swiss-Prot : SWS_FT_FI2 30) chain A residue 174 type BINDING sequence V description BINDING => ECO:0000269|PubMed:8512925 source Swiss-Prot : SWS_FT_FI2

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