eF-site ID 2act-A PDB Code 2act Chain A click to enlarge Title CRYSTALLOGRAPHIC REFINEMENT OF THE STRUCTURE OF ACTINIDIN AT 1.7 ANGSTROMS RESOLUTION BY FAST FOURIER LEAST-SQUARES METHODS Classification HYDROLASE (PROTEINASE) Compound ACTINIDIN PRECURSOR Source null (ACTN_ACTCH) Sequence A:  LPSYVDWRSAGAVVDIKSQGECGGXWAFSAIATVEGINKI TSGSLISLSEQELIDCGRTQNTRGCDGGYITDGFQFIIND GGINTEENYPYTAQDGDCDVALQDQKYVTIDTYENVPYNN EWALQTAVTYQPVSVALDAAGDAFKQYASGIFTGPCGTAV DHAIVIVGYGTEGGVDYWIVKNSWDTTWGEEGYMRILRNV GGAGTCGIATMPSYPVKY Description (1)  ACTINIDIN (SULFHYDRYL PROTEINASE) (E.C. NUMBER NOT ASSIGNED) Functional site 1) chain A residue 25 type sequence X description CATALYTIC RESIDUES AND THOSE INTIMATELY ASSOCIATED WITH THEM source : CAT 2) chain A residue 162 type sequence H description CATALYTIC RESIDUES AND THOSE INTIMATELY ASSOCIATED WITH THEM source : CAT 3) chain A residue 182 type sequence N description CATALYTIC RESIDUES AND THOSE INTIMATELY ASSOCIATED WITH THEM source : CAT 4) chain A residue 19 type sequence Q description CATALYTIC RESIDUES AND THOSE INTIMATELY ASSOCIATED WITH THEM source : CAT 5) chain A residue 184 type sequence W description CATALYTIC RESIDUES AND THOSE INTIMATELY ASSOCIATED WITH THEM source : CAT 6) chain A residue 69 type sequence Y description RESIDUES MAKING UP THE NON-POLAR BINDING POCKET FOR A SUBSTRATE (S2 SUB-SITE) source : S2 7) chain A residue 70 type sequence I description RESIDUES MAKING UP THE NON-POLAR BINDING POCKET FOR A SUBSTRATE (S2 SUB-SITE) source : S2 8) chain A residue 136 type sequence A description RESIDUES MAKING UP THE NON-POLAR BINDING POCKET FOR A SUBSTRATE (S2 SUB-SITE) source : S2 9) chain A residue 160 type sequence V description RESIDUES MAKING UP THE NON-POLAR BINDING POCKET FOR A SUBSTRATE (S2 SUB-SITE) source : S2 10) chain A residue 163 type sequence A description RESIDUES MAKING UP THE NON-POLAR BINDING POCKET FOR A SUBSTRATE (S2 SUB-SITE) source : S2 11) chain A residue 211 type sequence M description RESIDUES MAKING UP THE NON-POLAR BINDING POCKET FOR A SUBSTRATE (S2 SUB-SITE) source : S2 12) chain A residue 52 type sequence E description BINDING SITE FOR RESIDUE NH4 A 221 source : AC1 13) chain A residue 80 type sequence D description BINDING SITE FOR RESIDUE NH4 A 221 source : AC1 14) chain A residue 83 type sequence I description BINDING SITE FOR RESIDUE NH4 A 221 source : AC1 15) chain A residue 84 type sequence N description BINDING SITE FOR RESIDUE NH4 A 221 source : AC1 16) chain A residue 102 type sequence L description BINDING SITE FOR RESIDUE NH4 A 221 source : AC1 17) chain A residue 103 type sequence Q description BINDING SITE FOR RESIDUE NH4 A 221 source : AC1 18) chain A residue 105 type sequence Q description BINDING SITE FOR RESIDUE NH4 A 221 source : AC1 19) chain A residue 106 type sequence K description BINDING SITE FOR RESIDUE NH4 A 221 source : AC1 20) chain A residue 162 type ACT_SITE sequence H description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10089 source Swiss-Prot : SWS_FT_FI2 21) chain A residue 182 type ACT_SITE sequence N description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10090 source Swiss-Prot : SWS_FT_FI3 22) chain A residue 25 type BINDING sequence X description covalent => ECO:0000269|PubMed:1606141, ECO:0007744|PDB:1AEC source Swiss-Prot : SWS_FT_FI4 23) chain A residue 25 type ACT_SITE sequence X description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10088, ECO:0000305|PubMed:1606141, ECO:0007744|PDB:1AEC source Swiss-Prot : SWS_FT_FI1 24) chain A residue 19-30 type prosite sequence QGECGGXWAFSA description THIOL_PROTEASE_CYS Eukaryotic thiol (cysteine) proteases cysteine active site. QGeCGGCWAfSA source prosite : PS00139 25) chain A residue 160-170 type prosite sequence VDHAIVIVGYG description THIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. VDHAIVIVGYG source prosite : PS00639 26) chain A residue 177-196 type prosite sequence YWIVKNSWDTTWGEEGYMRI description THIOL_PROTEASE_ASN Eukaryotic thiol (cysteine) proteases asparagine active site. YWIvKNSWdttWGeeGYMrI source prosite : PS00640

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