eF-site ID 1bav-C PDB Code 1bav Chain C 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 C:  ARSTNTFNYATYHTLDEIYDFMDLLVAQHPELVSKLQIGR SYEGRPIYVLKFSTGGSNRPAIWIDLGIHSREWITQATGV WFAKKFTENYGQNPSFTAILDSMDIFLEIVTNPNGFAFTH SENRLWRKTRSVTSSSLCVGVDANRNWDAGFGKAGASSSP CSETYHGKYANSEVEVKSIVDFVKNHGNFKAFLSIHSYSQ LLLYPYGYTTQSIPDKTELNQVAKSAVAALKSLYGTSYKY GSIITTIYQASGGSIDWSYNQGIKYSFTFELRDTGRYGFL LPASQIIPTAQETWLGVLTIMEHTVNN Description (1)  CARBOXYPEPTIDASE A, 2-BENZYL-3-IODOPROPANOIC ACID Functional site 1) chain C residue 69 type sequence H description BINDING SITE FOR RESIDUE ZN C 310 source : AC3 2) chain C residue 72 type sequence E description BINDING SITE FOR RESIDUE ZN C 310 source : AC3 3) chain C residue 196 type sequence H description BINDING SITE FOR RESIDUE ZN C 310 source : AC3 4) chain C residue 69 type sequence H description BINDING SITE FOR RESIDUE BIP C 311 source : AC7 5) chain C residue 144 type sequence N description BINDING SITE FOR RESIDUE BIP C 311 source : AC7 6) chain C residue 145 type sequence R description BINDING SITE FOR RESIDUE BIP C 311 source : AC7 7) chain C residue 196 type sequence H description BINDING SITE FOR RESIDUE BIP C 311 source : AC7 8) chain C residue 247 type sequence I description BINDING SITE FOR RESIDUE BIP C 311 source : AC7 9) chain C residue 248 type sequence Y description BINDING SITE FOR RESIDUE BIP C 311 source : AC7 10) chain C residue 268 type sequence T description BINDING SITE FOR RESIDUE BIP C 311 source : AC7 11) chain C residue 270 type sequence E description BINDING SITE FOR RESIDUE BIP C 311 source : AC7 12) chain C residue 69 type catalytic sequence H description 171 source MCSA : MCSA3 13) chain C residue 72 type catalytic sequence E description 171 source MCSA : MCSA3 14) chain C residue 127 type catalytic sequence R description 171 source MCSA : MCSA3 15) chain C residue 196 type catalytic sequence H description 171 source MCSA : MCSA3 16) chain C residue 270 type catalytic sequence E description 171 source MCSA : MCSA3 17) chain C residue 144 type BINDING sequence N description BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 source Swiss-Prot : SWS_FT_FI3 18) chain C residue 197 type BINDING sequence S description BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 source Swiss-Prot : SWS_FT_FI3 19) chain C residue 248 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 source Swiss-Prot : SWS_FT_FI3 20) chain C residue 127 type BINDING sequence R description BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 source Swiss-Prot : SWS_FT_FI3 21) chain C residue 270 type ACT_SITE sequence E description Proton donor/acceptor => ECO:0000255|PROSITE-ProRule:PRU01379 source Swiss-Prot : SWS_FT_FI1 22) chain C 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 23) chain C 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 24) chain C 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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