eF-site ID 1bav-B PDB Code 1bav Chain B 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 B:  ARSTNTFNYATYHTLDEIYDFMDLLVAQHPELVSKLQIGR SYEGRPIYVLKFSTGGSNRPAIWIDLGIHSREWITQATGV WFAKKFTENYGQNPSFTAILDSMDIFLEIVTNPNGFAFTH SENRLWRKTRSVTSSSLCVGVDANRNWDAGFGKAGASSSP CSETYHGKYANSEVEVKSIVDFVKNHGNFKAFLSIHSYSQ LLLYPYGYTTQSIPDKTELNQVAKSAVAALKSLYGTSYKY GSIITTIYQASGGSIDWSYNQGIKYSFTFELRDTGRYGFL LPASQIIPTAQETWLGVLTIMEHTVNN Description Functional site 1) chain B residue 69 type sequence H description BINDING SITE FOR RESIDUE ZN B 310 source : AC2 2) chain B residue 72 type sequence E description BINDING SITE FOR RESIDUE ZN B 310 source : AC2 3) chain B residue 196 type sequence H description BINDING SITE FOR RESIDUE ZN B 310 source : AC2 4) chain B residue 69 type sequence H description BINDING SITE FOR RESIDUE BIP B 311 source : AC6 5) chain B residue 127 type sequence R description BINDING SITE FOR RESIDUE BIP B 311 source : AC6 6) chain B residue 144 type sequence N description BINDING SITE FOR RESIDUE BIP B 311 source : AC6 7) chain B residue 145 type sequence R description BINDING SITE FOR RESIDUE BIP B 311 source : AC6 8) chain B residue 196 type sequence H description BINDING SITE FOR RESIDUE BIP B 311 source : AC6 9) chain B residue 243 type sequence I description BINDING SITE FOR RESIDUE BIP B 311 source : AC6 10) chain B residue 250 type sequence A description BINDING SITE FOR RESIDUE BIP B 311 source : AC6 11) chain B residue 268 type sequence T description BINDING SITE FOR RESIDUE BIP B 311 source : AC6 12) chain B residue 270 type sequence E description BINDING SITE FOR RESIDUE BIP B 311 source : AC6 13) chain B residue 69 type catalytic sequence H description 171 source MCSA : MCSA2 14) chain B residue 72 type catalytic sequence E description 171 source MCSA : MCSA2 15) chain B residue 127 type catalytic sequence R description 171 source MCSA : MCSA2 16) chain B residue 196 type catalytic sequence H description 171 source MCSA : MCSA2 17) chain B residue 270 type catalytic sequence E description 171 source MCSA : MCSA2 18) chain B residue 270 type ACT_SITE sequence E description Proton donor/acceptor => ECO:0000255|PROSITE-ProRule:PRU01379 source Swiss-Prot : SWS_FT_FI1 19) chain B 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 20) chain B 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 21) chain B 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 22) chain B residue 127 type BINDING sequence R description BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 source Swiss-Prot : SWS_FT_FI3 23) chain B residue 144 type BINDING sequence N description BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 source Swiss-Prot : SWS_FT_FI3 24) chain B residue 197 type BINDING sequence S description BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 source Swiss-Prot : SWS_FT_FI3 25) chain B residue 248 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 source Swiss-Prot : SWS_FT_FI3

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