eF-site ID 2abz-ABCDEF PDB Code 2abz Chain A, B, C, D, E, F click to enlarge Title Crystal structure of C19A/C43A mutant of leech carboxypeptidase inhibitor in complex with bovine carboxypeptidase A Classification hydrolase/hydrolase inhibitor Compound Carboxypeptidase A1 Source Bos taurus (Bovine) (MCPI_HIRME) Sequence A:  TNTFNYATYHTLDEIYDFMDLLVAEHPQLVSKLQIGRSYE GRPIYVLKFSTGGSNRPAIWIDLGIHSREWITQATGVWFA KKFTEDYGQDPSFTAILDSMDIFLEIVTNPDGFAFTHSQN RLWRKTRSVSLCVGVDANRNWDAGFGKAGASSSPCSETYH GKYANSEVEVKSIVDFVKDHGNFKAFLSIHSYSQLLLYPY GYTTQSIPDKTELNQVAKSAVAALKSLYGTSYKYGSIITT IYQASGGSIDWSYNQGIKYSFTFELRDTGRYGFLLPASQI IPTAQETWLGVLTIMEHTV B:  STNTFNYATYHTLDEIYDFMDLLVAEHPQLVSKLQIGRSY EGRPIYVLKFSTGGSNRPAIWIDLGIHSREWITQATGVWF AKKFTEDYGQDPSFTAILDSMDIFLEIVTNPDGFAFTHSQ NRLWRKTRSVTSLCVGVDANRNWDAGFGKAGASSSPCSET YHGKYANSEVEVKSIVDFVKDHGNFKAFLSIHSYSQLLLY PYGYTTQSIPDKTELNQVAKSAVAALKSLYGTSYKYGSII TTIYQASGGSIDWSYNQGIKYSFTFELRDTGRYGFLLPAS QIIPTAQETWLGVLTIMEHTV C:  PDESFLCYQPDQVCAFICRGAAPLPSEGECNPHPTAPWAR EGAVEWVPYSTGQCRTTCIPYV D:  TPDESFLCYDQVCFICRGAAPLPEGECNPHPTAPWASTGQ CRTTCI E:  DESFLCYQPDQVCAFICRGAAPLPSEGECNPHPTAPWARE GAVEWVPYTGQCRTTCIPYV F:  TPDESFLCYQPDQVCAFICRGAAPLPSEGECNPHPTAPWA RVEWVPTGQCRTTCIPYV Description Functional site 1) chain A residue 69 type sequence H description BINDING SITE FOR RESIDUE ZN A 1001 source : AC1 2) chain A residue 72 type sequence E description BINDING SITE FOR RESIDUE ZN A 1001 source : AC1 3) chain A residue 196 type sequence H description BINDING SITE FOR RESIDUE ZN A 1001 source : AC1 4) chain C residue 66 type sequence V description BINDING SITE FOR RESIDUE ZN A 1001 source : AC1 5) chain B residue 69 type sequence H description BINDING SITE FOR RESIDUE ZN B 1002 source : AC2 6) chain B residue 72 type sequence E description BINDING SITE FOR RESIDUE ZN B 1002 source : AC2 7) chain B residue 196 type sequence H description BINDING SITE FOR RESIDUE ZN B 1002 source : AC2 8) chain E residue 66 type sequence V description BINDING SITE FOR RESIDUE ZN B 1002 source : AC2 9) chain A residue 69 type catalytic sequence H description 171 source MCSA : MCSA1 10) chain A residue 72 type catalytic sequence E description 171 source MCSA : MCSA1 11) chain A residue 127 type catalytic sequence R description 171 source MCSA : MCSA1 12) chain A residue 196 type catalytic sequence H description 171 source MCSA : MCSA1 13) chain A residue 270 type catalytic sequence E description 171 source MCSA : MCSA1 14) chain B residue 69 type catalytic sequence H description 171 source MCSA : MCSA2 15) chain B residue 72 type catalytic sequence E description 171 source MCSA : MCSA2 16) chain B residue 127 type catalytic sequence R description 171 source MCSA : MCSA2 17) chain B residue 196 type catalytic sequence H description 171 source MCSA : MCSA2 18) chain B residue 270 type catalytic sequence E description 171 source MCSA : MCSA2 19) chain A residue 60-82 type prosite sequence PAIWIDLGIHSREWITQATGVWF description CARBOXYPEPT_ZN_1 Zinc carboxypeptidases, zinc-binding region 1 signature. PaIwIdlGiHSrEwITQatgvwF source prosite : PS00132 20) chain A residue 196-206 type prosite sequence HSYSQLLLYPY description CARBOXYPEPT_ZN_2 Zinc carboxypeptidases, zinc-binding region 2 signature. HSYSQLLlYPY source prosite : PS00133 21) chain C residue 66 type SITE sequence V description Interaction with carboxypeptidase => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 22) chain E residue 66 type SITE sequence V description Interaction with carboxypeptidase => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 23) chain F residue 66 type SITE sequence V description Interaction with carboxypeptidase => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 24) chain A residue 127 type BINDING sequence R description BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 source Swiss-Prot : SWS_FT_FI3 25) chain A residue 144 type BINDING sequence N description BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 source Swiss-Prot : SWS_FT_FI3 26) chain A residue 197 type BINDING sequence S description BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 source Swiss-Prot : SWS_FT_FI3 27) chain A residue 248 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 source Swiss-Prot : SWS_FT_FI3 28) chain B residue 127 type BINDING sequence R description BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 source Swiss-Prot : SWS_FT_FI3 29) chain B residue 144 type BINDING sequence N description BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 source Swiss-Prot : SWS_FT_FI3 30) chain B residue 197 type BINDING sequence S description BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 source Swiss-Prot : SWS_FT_FI3 31) chain B residue 248 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 source Swiss-Prot : SWS_FT_FI3 32) 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 33) 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 34) 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 35) 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 36) 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 37) 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

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