eF-site ID 1arl-A PDB Code 1arl Chain A click to enlarge Title CARBOXYPEPTIDASE A WITH ZN REMOVED Classification CARBOXYPEPTIDASE Compound APO-CARBOXYPEPTIDASE A=ALPHA= (COX) Source ORGANISM_COMMON: cattle; ORGANISM_SCIENTIFIC: Bos taurus; Sequence A:  ARSTNTFNYATYHTLDEIYDFMDLLVAEHPQLVSKLQIGR SYEGRPIYVLKFSTGGSNRPAIWIDLGIHSREWITQATGV WFAKKFTEDYGQDPSFTAILDSMDIFLEIVTNPDGFAFTH SQNRLWRKTRSVTSSSLCVGVDANRNWDAGFGKAGASSSP CSETYHGKYANSEVEVKSIVDFVKDHGNFKAFLSIHSYSQ LLLYPYGYTTQSIPDKTELNQVAKSAVAALKSLYGTSYKY GSIITTIYQASGGSIDWSYNQGIKYSFTFELRDTGRYGFL LPASQIIPTAQETWLGVLTIMEHTVNN Description (1)  APO-CARBOXYPEPTIDASE A ALPHA (COX) Functional site 1) chain A residue 69 type catalytic sequence H description 171 source MCSA : MCSA1 2) chain A residue 72 type catalytic sequence E description 171 source MCSA : MCSA1 3) chain A residue 127 type catalytic sequence R description 171 source MCSA : MCSA1 4) chain A residue 196 type catalytic sequence H description 171 source MCSA : MCSA1 5) chain A residue 270 type catalytic sequence E description 171 source MCSA : MCSA1 6) chain A residue 60-82 type prosite sequence PAIWIDLGIHSREWITQATGVWF description CARBOXYPEPT_ZN_1 Zinc carboxypeptidases, zinc-binding region 1 signature. PaIwIdlGiHSrEwITQatgvwF source prosite : PS00132 7) chain A residue 196-206 type prosite sequence HSYSQLLLYPY description CARBOXYPEPT_ZN_2 Zinc carboxypeptidases, zinc-binding region 2 signature. HSYSQLLlYPY source prosite : PS00133 8) chain A residue 127 type BINDING sequence R description BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 source Swiss-Prot : SWS_FT_FI3 9) chain A residue 144 type BINDING sequence N description BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 source Swiss-Prot : SWS_FT_FI3 10) chain A residue 197 type BINDING sequence S description BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 source Swiss-Prot : SWS_FT_FI3 11) chain A residue 248 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 source Swiss-Prot : SWS_FT_FI3 12) chain A residue 270 type ACT_SITE sequence E description Proton donor/acceptor => ECO:0000255|PROSITE-ProRule:PRU01379 source Swiss-Prot : SWS_FT_FI1 13) chain A residue 69 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU01379, ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 source Swiss-Prot : SWS_FT_FI2 14) chain A residue 72 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU01379, ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 source Swiss-Prot : SWS_FT_FI2 15) chain A residue 196 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU01379, ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 source Swiss-Prot : SWS_FT_FI2

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