eF-site ID 1iy7-A PDB Code 1iy7 Chain A click to enlarge Title Crystal Structure of CPA and sulfamide-based inhibitor complex Classification HYDROLASE Compound Carboxypeptidase A Source Bos taurus (Bovine) (CBPA1_BOVIN) Sequence A:  ARSTNTFNYATYHTLDEIYDFMDLLVAQHPELVSKLQIGR SYEGRPIYVLKFSTGGSNRPAIWIDLGIHSREWITQATGV WFAKKFTENYGQNPSFTAILDSMDIFLEIVTNPNGFAFTH SENRLWRKTRSVTSSSLCVGVDANRNWDAGFGKAGASSSP CSETYHGKYANSEVEVKSIVDFVKNHGNFKAFLSIHSYSQ LLLYPYGYTTQSIPDKTELNQVAKSAVAALKSLYGTSYKY GSIITTIYQASGGSIDWSYNQGIKYSFTFELRDTGRYGFL LPASQIIPTAQETWLGVLTIMEHTVNN Description Functional site 1) chain A residue 69 type sequence H description BINDING SITE FOR RESIDUE ZN A 308 source : AC1 2) chain A residue 72 type sequence E description BINDING SITE FOR RESIDUE ZN A 308 source : AC1 3) chain A residue 196 type sequence H description BINDING SITE FOR RESIDUE ZN A 308 source : AC1 4) chain A residue 69 type sequence H description BINDING SITE FOR RESIDUE CXA A 500 source : AC2 5) chain A residue 72 type sequence E description BINDING SITE FOR RESIDUE CXA A 500 source : AC2 6) chain A residue 127 type sequence R description BINDING SITE FOR RESIDUE CXA A 500 source : AC2 7) chain A residue 144 type sequence N description BINDING SITE FOR RESIDUE CXA A 500 source : AC2 8) chain A residue 145 type sequence R description BINDING SITE FOR RESIDUE CXA A 500 source : AC2 9) chain A residue 196 type sequence H description BINDING SITE FOR RESIDUE CXA A 500 source : AC2 10) chain A residue 197 type sequence S description BINDING SITE FOR RESIDUE CXA A 500 source : AC2 11) chain A residue 243 type sequence I description BINDING SITE FOR RESIDUE CXA A 500 source : AC2 12) chain A residue 248 type sequence Y description BINDING SITE FOR RESIDUE CXA A 500 source : AC2 13) chain A residue 268 type sequence T description BINDING SITE FOR RESIDUE CXA A 500 source : AC2 14) chain A residue 270 type sequence E description BINDING SITE FOR RESIDUE CXA A 500 source : AC2 15) chain A residue 69 type catalytic sequence H description 171 source MCSA : MCSA1 16) chain A residue 72 type catalytic sequence E description 171 source MCSA : MCSA1 17) chain A residue 127 type catalytic sequence R description 171 source MCSA : MCSA1 18) chain A residue 196 type catalytic sequence H description 171 source MCSA : MCSA1 19) chain A residue 270 type catalytic sequence E description 171 source MCSA : MCSA1 20) chain A residue 60-82 type prosite sequence PAIWIDLGIHSREWITQATGVWF description CARBOXYPEPT_ZN_1 Zinc carboxypeptidases, zinc-binding region 1 signature. PaIwIdlGiHSrEwITQatgvwF source prosite : PS00132 21) chain A residue 196-206 type prosite sequence HSYSQLLLYPY description CARBOXYPEPT_ZN_2 Zinc carboxypeptidases, zinc-binding region 2 signature. HSYSQLLlYPY source prosite : PS00133 22) chain A residue 127 type BINDING sequence R description BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 source Swiss-Prot : SWS_FT_FI3 23) chain A residue 144 type BINDING sequence N description BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 source Swiss-Prot : SWS_FT_FI3 24) chain A residue 197 type BINDING sequence S description BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 source Swiss-Prot : SWS_FT_FI3 25) chain A residue 248 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 source Swiss-Prot : SWS_FT_FI3 26) chain A residue 270 type ACT_SITE sequence E description Proton donor/acceptor => ECO:0000255|PROSITE-ProRule:PRU01379 source Swiss-Prot : SWS_FT_FI1 27) 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 28) 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 29) 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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