eF-site ID 1aye-A PDB Code 1aye Chain A click to enlarge Title HUMAN PROCARBOXYPEPTIDASE A2 Classification SERINE PROTEASE Compound PROCARBOXYPEPTIDASE A2 Source null (CPB2_HUMAN) Sequence A:  LETFVGDQVLEIVPSNEEQIKNLLQLEAQEHLQLDFWKSP TTPGETAHVRVPFVNVQAVKVFLESQGIAYSIMIEDVQVL LDKENEEMLFNRRRERSGNFNFGAYHTLEEISQEMDNLVA EHPGLVSKVNIGSSFENRPMNVLKFSTGGDKPAIWLDAGI HAREWVTQATALWTANKIVSDYGKDPSITSILDALDIFLL PVTNPDGYVFSQTKNRMWRKTRSKVSGSLCVGVDPNRNWD AGFGGPGASSNPCSDSYHGPSANSEVEVKSIVDFIKSHGK VKAFIILHSYSQLLMFPYGYKCTKLDDFDELSEVAQKAAQ SLRSLHGTKYKVGPICSVIYQASGGSIDWSYDYGIKYSFA FELRDTGRYGFLLPARQILPTAEETWLGLKAIMEHVRDHP Y Description Functional site 1) chain A residue 145 type sequence R description source : S0 2) chain A residue 144 type sequence N description source : S0 3) chain A residue 248 type sequence Y description source : S0 4) chain A residue 127 type sequence R description source : S1 5) chain A residue 270 type sequence E description source : S1 6) chain A residue 71 type sequence R description source : S2 7) chain A residue 197 type sequence S description source : S2 8) chain A residue 198 type sequence Y description source : S2 9) chain A residue 199 type sequence S description source : S2 10) chain A residue 279 type sequence F description source : S3 11) chain A residue 122 type sequence K description source : S4 12) chain A residue 124 type sequence R description source : S4 13) chain A residue 128 type sequence K description source : S4 14) chain A residue 69 type sequence H description BINDING SITE FOR RESIDUE ZN A 400 source : AC1 15) chain A residue 72 type sequence E description BINDING SITE FOR RESIDUE ZN A 400 source : AC1 16) chain A residue 196 type sequence H description BINDING SITE FOR RESIDUE ZN A 400 source : AC1 17) chain A residue 272 type ACT_SITE sequence R description Proton donor/acceptor => ECO:0000255|PROSITE-ProRule:PRU01379 source Swiss-Prot : SWS_FT_FI1 18) chain A residue 71 type BINDING sequence R description BINDING => ECO:0000255|PROSITE-ProRule:PRU01379, ECO:0000269|PubMed:10742178, ECO:0000269|PubMed:9384570 source Swiss-Prot : SWS_FT_FI2 19) chain A residue 74 type BINDING sequence V description BINDING => ECO:0000255|PROSITE-ProRule:PRU01379, ECO:0000269|PubMed:10742178, ECO:0000269|PubMed:9384570 source Swiss-Prot : SWS_FT_FI2 20) chain A residue 198 type BINDING sequence Y description BINDING => ECO:0000255|PROSITE-ProRule:PRU01379, ECO:0000269|PubMed:10742178, ECO:0000269|PubMed:9384570 source Swiss-Prot : SWS_FT_FI2 21) chain A residue 129 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P00730 source Swiss-Prot : SWS_FT_FI3 22) chain A residue 146 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P00730 source Swiss-Prot : SWS_FT_FI3 23) chain A residue 199 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P00730 source Swiss-Prot : SWS_FT_FI3 24) chain A residue 250 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P00730 source Swiss-Prot : SWS_FT_FI3 25) chain A residue 60-82 type prosite sequence PAIWLDAGIHAREWVTQATALWT description CARBOXYPEPT_ZN_1 Zinc carboxypeptidases, zinc-binding region 1 signature. PaIwLdaGiHArEwVTQatalwT source prosite : PS00132 26) chain A residue 196-206 type prosite sequence HSYSQLLMFPY description CARBOXYPEPT_ZN_2 Zinc carboxypeptidases, zinc-binding region 2 signature. HSYSQLLmFPY source prosite : PS00133

Display surface Download Links