eF-site ID 1avt-A PDB Code 1avt Chain A click to enlarge Title SUBTILISIN CARLSBERG D-PARA-CHLOROPHENYL-1-ACETAMIDO BORONIC ACID INHIBITOR COMPLEX Classification SERINE PROTEASE Compound SUBTILISIN CARLSBERG, TYPE VIII Source ORGANISM_SCIENTIFIC: Bacillus licheniformis; Sequence A:  AQTVPYGIPLIKADKVQAQGFKGANVKVAVLDTGIQASHP DLNVVGGASFVAGEAYNTDGNGHGTHVAGTVAALDNTTGV LGVAPSVSLYAVKVLNSSGSGSYSGIVSGIEWATTNGMDV INMSLGGASGSTAMKQAVDNAYARGVVVVAAAGNSGNSGS TNTIGYPAKYDSVIAVGAVDSNSNRASFSSVGAELEVMAP GAGVYSTYPTNTYATLNGTXMASPHVAGAAALILSKHPNL SASQVRNRLSSTATYLGSSFYYGKGLINVEAAAQ Description Functional site 1) chain A residue 32 type sequence D description SERINE OF THE ACTIVE SITE HAS BEEN CHEMICALLY MODIFIED TO INCLUDE A COVALENT BOND FROM OG TO BORON OF THE INHIBITOR. source : ACT 2) chain A residue 64 type sequence H description SERINE OF THE ACTIVE SITE HAS BEEN CHEMICALLY MODIFIED TO INCLUDE A COVALENT BOND FROM OG TO BORON OF THE INHIBITOR. source : ACT 3) chain A residue 221 type sequence X description SERINE OF THE ACTIVE SITE HAS BEEN CHEMICALLY MODIFIED TO INCLUDE A COVALENT BOND FROM OG TO BORON OF THE INHIBITOR. source : ACT 4) chain A residue 75 type sequence L description CALCIUM METAL BINDING SITE 1. source : M1 5) chain A residue 77 type sequence N description CALCIUM METAL BINDING SITE 1. source : M1 6) chain A residue 79 type sequence T description CALCIUM METAL BINDING SITE 1. source : M1 7) chain A residue 81 type sequence V description CALCIUM METAL BINDING SITE 1. source : M1 8) chain A residue 169 type sequence A description CALCIUM METAL BINDING SITE 2. source : M2 9) chain A residue 174 type sequence V description CALCIUM METAL BINDING SITE 2. source : M2 10) chain A residue 169 type sequence A description BINDING SITE FOR RESIDUE NA A 300 source : AC1 11) chain A residue 171 type sequence Y description BINDING SITE FOR RESIDUE NA A 300 source : AC1 12) chain A residue 174 type sequence V description BINDING SITE FOR RESIDUE NA A 300 source : AC1 13) chain A residue 2 type sequence Q description BINDING SITE FOR RESIDUE NA A 301 source : AC2 14) chain A residue 41 type sequence D description BINDING SITE FOR RESIDUE NA A 301 source : AC2 15) chain A residue 75 type sequence L description BINDING SITE FOR RESIDUE NA A 301 source : AC2 16) chain A residue 77 type sequence N description BINDING SITE FOR RESIDUE NA A 301 source : AC2 17) chain A residue 79 type sequence T description BINDING SITE FOR RESIDUE NA A 301 source : AC2 18) chain A residue 81 type sequence V description BINDING SITE FOR RESIDUE NA A 301 source : AC2 19) chain A residue 28-39 type prosite sequence VAVLDTGIQASH description SUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. VAVLDTGIqasH source prosite : PS00136 20) chain A residue 64-74 type prosite sequence HGTHVAGTVAA description SUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGThVAGtVAA source prosite : PS00137 21) chain A residue 32 type ACT_SITE sequence D description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240 source Swiss-Prot : SWS_FT_FI1 22) chain A residue 64 type ACT_SITE sequence H description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240 source Swiss-Prot : SWS_FT_FI1 23) chain A residue 221 type ACT_SITE sequence X description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240 source Swiss-Prot : SWS_FT_FI1 24) chain A residue 2 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:8512925 source Swiss-Prot : SWS_FT_FI2 25) chain A residue 41 type BINDING sequence D description BINDING => ECO:0000269|PubMed:8512925 source Swiss-Prot : SWS_FT_FI2 26) chain A residue 75 type BINDING sequence L description BINDING => ECO:0000269|PubMed:8512925 source Swiss-Prot : SWS_FT_FI2 27) chain A residue 77 type BINDING sequence N description BINDING => ECO:0000269|PubMed:8512925 source Swiss-Prot : SWS_FT_FI2 28) chain A residue 79 type BINDING sequence T description BINDING => ECO:0000269|PubMed:8512925 source Swiss-Prot : SWS_FT_FI2 29) chain A residue 81 type BINDING sequence V description BINDING => ECO:0000269|PubMed:8512925 source Swiss-Prot : SWS_FT_FI2 30) chain A residue 169 type BINDING sequence A description BINDING => ECO:0000269|PubMed:8512925 source Swiss-Prot : SWS_FT_FI2 31) chain A residue 171 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:8512925 source Swiss-Prot : SWS_FT_FI2 32) chain A residue 174 type BINDING sequence V description BINDING => ECO:0000269|PubMed:8512925 source Swiss-Prot : SWS_FT_FI2

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