eF-site ID 1bav-A PDB Code 1bav Chain A click to enlarge Title CARBOXYPEPTIDASE A COMPLEXED WITH 2-BENZYL-3-IODO-PROPANOIC ACID (BIP) Classification CARBOXYPEPTIDASE Compound CARBOXYPEPTIDASE A Source ORGANISM_COMMON: cattle; ORGANISM_SCIENTIFIC: Bos taurus; Sequence A:  ARSTNTFNYATYHTLDEIYDFMDLLVAQHPELVSKLQIGR SYEGRPIYVLKFSTGGSNRPAIWIDLGIHSREWITQATGV WFAKKFTENYGQNPSFTAILDSMDIFLEIVTNPNGFAFTH SENRLWRKTRSVTSSSLCVGVDANRNWDAGFGKAGASSSP CSETYHGKYANSEVEVKSIVDFVKNHGNFKAFLSIHSYSQ LLLYPYGYTTQSIPDKTELNQVAKSAVAALKSLYGTSYKY GSIITTIYQASGGSIDWSYNQGIKYSFTFELRDTGRYGFL LPASQIIPTAQETWLGVLTIMEHTVNN Description (1)  CARBOXYPEPTIDASE A, 2-BENZYL-3-IODOPROPANOIC ACID Functional site 1) chain A residue 69 type sequence H description BINDING SITE FOR RESIDUE ZN A 310 source : AC1 2) chain A residue 72 type sequence E description BINDING SITE FOR RESIDUE ZN A 310 source : AC1 3) chain A residue 196 type sequence H description BINDING SITE FOR RESIDUE ZN A 310 source : AC1 4) chain A residue 69 type sequence H description BINDING SITE FOR RESIDUE BIP A 311 source : AC5 5) chain A residue 144 type sequence N description BINDING SITE FOR RESIDUE BIP A 311 source : AC5 6) chain A residue 145 type sequence R description BINDING SITE FOR RESIDUE BIP A 311 source : AC5 7) chain A residue 196 type sequence H description BINDING SITE FOR RESIDUE BIP A 311 source : AC5 8) chain A residue 203 type sequence L description BINDING SITE FOR RESIDUE BIP A 311 source : AC5 9) chain A residue 243 type sequence I description BINDING SITE FOR RESIDUE BIP A 311 source : AC5 10) chain A residue 247 type sequence I description BINDING SITE FOR RESIDUE BIP A 311 source : AC5 11) chain A residue 248 type sequence Y description BINDING SITE FOR RESIDUE BIP A 311 source : AC5 12) chain A residue 270 type sequence E description BINDING SITE FOR RESIDUE BIP A 311 source : AC5 13) chain A residue 69 type catalytic sequence H description 171 source MCSA : MCSA1 14) chain A residue 72 type catalytic sequence E description 171 source MCSA : MCSA1 15) chain A residue 127 type catalytic sequence R description 171 source MCSA : MCSA1 16) chain A residue 196 type catalytic sequence H description 171 source MCSA : MCSA1 17) chain A residue 270 type catalytic sequence E description 171 source MCSA : MCSA1 18) chain A residue 60-82 type prosite sequence PAIWIDLGIHSREWITQATGVWF description CARBOXYPEPT_ZN_1 Zinc carboxypeptidases, zinc-binding region 1 signature. PaIwIdlGiHSrEwITQatgvwF source prosite : PS00132 19) chain A residue 196-206 type prosite sequence HSYSQLLLYPY description CARBOXYPEPT_ZN_2 Zinc carboxypeptidases, zinc-binding region 2 signature. HSYSQLLlYPY source prosite : PS00133 20) chain A residue 127 type BINDING sequence R description BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 source Swiss-Prot : SWS_FT_FI3 21) chain A residue 144 type BINDING sequence N description BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 source Swiss-Prot : SWS_FT_FI3 22) chain A residue 197 type BINDING sequence S description BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 source Swiss-Prot : SWS_FT_FI3 23) chain A residue 248 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 source Swiss-Prot : SWS_FT_FI3 24) chain A residue 270 type ACT_SITE sequence E description Proton donor/acceptor => ECO:0000255|PROSITE-ProRule:PRU01379 source Swiss-Prot : SWS_FT_FI1 25) 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 26) 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 27) 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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