eF-site ID 1bav-ABCD PDB Code 1bav Chain A, B, C, D 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 B:  ARSTNTFNYATYHTLDEIYDFMDLLVAQHPELVSKLQIGR SYEGRPIYVLKFSTGGSNRPAIWIDLGIHSREWITQATGV WFAKKFTENYGQNPSFTAILDSMDIFLEIVTNPNGFAFTH SENRLWRKTRSVTSSSLCVGVDANRNWDAGFGKAGASSSP CSETYHGKYANSEVEVKSIVDFVKNHGNFKAFLSIHSYSQ LLLYPYGYTTQSIPDKTELNQVAKSAVAALKSLYGTSYKY GSIITTIYQASGGSIDWSYNQGIKYSFTFELRDTGRYGFL LPASQIIPTAQETWLGVLTIMEHTVNN C:  ARSTNTFNYATYHTLDEIYDFMDLLVAQHPELVSKLQIGR SYEGRPIYVLKFSTGGSNRPAIWIDLGIHSREWITQATGV WFAKKFTENYGQNPSFTAILDSMDIFLEIVTNPNGFAFTH SENRLWRKTRSVTSSSLCVGVDANRNWDAGFGKAGASSSP CSETYHGKYANSEVEVKSIVDFVKNHGNFKAFLSIHSYSQ LLLYPYGYTTQSIPDKTELNQVAKSAVAALKSLYGTSYKY GSIITTIYQASGGSIDWSYNQGIKYSFTFELRDTGRYGFL LPASQIIPTAQETWLGVLTIMEHTVNN D:  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 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 B residue 69 type sequence H description BINDING SITE FOR RESIDUE ZN B 310 source : AC2 5) chain B residue 72 type sequence E description BINDING SITE FOR RESIDUE ZN B 310 source : AC2 6) chain B residue 196 type sequence H description BINDING SITE FOR RESIDUE ZN B 310 source : AC2 7) chain C residue 69 type sequence H description BINDING SITE FOR RESIDUE ZN C 310 source : AC3 8) chain C residue 72 type sequence E description BINDING SITE FOR RESIDUE ZN C 310 source : AC3 9) chain C residue 196 type sequence H description BINDING SITE FOR RESIDUE ZN C 310 source : AC3 10) chain D residue 69 type sequence H description BINDING SITE FOR RESIDUE ZN D 310 source : AC4 11) chain D residue 72 type sequence E description BINDING SITE FOR RESIDUE ZN D 310 source : AC4 12) chain D residue 196 type sequence H description BINDING SITE FOR RESIDUE ZN D 310 source : AC4 13) chain A residue 69 type sequence H description BINDING SITE FOR RESIDUE BIP A 311 source : AC5 14) chain A residue 144 type sequence N description BINDING SITE FOR RESIDUE BIP A 311 source : AC5 15) chain A residue 145 type sequence R description BINDING SITE FOR RESIDUE BIP A 311 source : AC5 16) chain A residue 196 type sequence H description BINDING SITE FOR RESIDUE BIP A 311 source : AC5 17) chain A residue 203 type sequence L description BINDING SITE FOR RESIDUE BIP A 311 source : AC5 18) chain A residue 243 type sequence I description BINDING SITE FOR RESIDUE BIP A 311 source : AC5 19) chain A residue 247 type sequence I description BINDING SITE FOR RESIDUE BIP A 311 source : AC5 20) chain A residue 248 type sequence Y description BINDING SITE FOR RESIDUE BIP A 311 source : AC5 21) chain A residue 270 type sequence E description BINDING SITE FOR RESIDUE BIP A 311 source : AC5 22) chain B residue 69 type sequence H description BINDING SITE FOR RESIDUE BIP B 311 source : AC6 23) chain B residue 127 type sequence R description BINDING SITE FOR RESIDUE BIP B 311 source : AC6 24) chain B residue 144 type sequence N description BINDING SITE FOR RESIDUE BIP B 311 source : AC6 25) chain B residue 145 type sequence R description BINDING SITE FOR RESIDUE BIP B 311 source : AC6 26) chain B residue 196 type sequence H description BINDING SITE FOR RESIDUE BIP B 311 source : AC6 27) chain B residue 243 type sequence I description BINDING SITE FOR RESIDUE BIP B 311 source : AC6 28) chain B residue 250 type sequence A description BINDING SITE FOR RESIDUE BIP B 311 source : AC6 29) chain B residue 268 type sequence T description BINDING SITE FOR RESIDUE BIP B 311 source : AC6 30) chain B residue 270 type sequence E description BINDING SITE FOR RESIDUE BIP B 311 source : AC6 31) chain C residue 69 type sequence H description BINDING SITE FOR RESIDUE BIP C 311 source : AC7 32) chain C residue 144 type sequence N description BINDING SITE FOR RESIDUE BIP C 311 source : AC7 33) chain C residue 145 type sequence R description BINDING SITE FOR RESIDUE BIP C 311 source : AC7 34) chain C residue 196 type sequence H description BINDING SITE FOR RESIDUE BIP C 311 source : AC7 35) chain C residue 247 type sequence I description BINDING SITE FOR RESIDUE BIP C 311 source : AC7 36) chain C residue 248 type sequence Y description BINDING SITE FOR RESIDUE BIP C 311 source : AC7 37) chain C residue 268 type sequence T description BINDING SITE FOR RESIDUE BIP C 311 source : AC7 38) chain C residue 270 type sequence E description BINDING SITE FOR RESIDUE BIP C 311 source : AC7 39) chain D residue 69 type sequence H description BINDING SITE FOR RESIDUE BIP D 311 source : AC8 40) chain D residue 144 type sequence N description BINDING SITE FOR RESIDUE BIP D 311 source : AC8 41) chain D residue 145 type sequence R description BINDING SITE FOR RESIDUE BIP D 311 source : AC8 42) chain D residue 196 type sequence H description BINDING SITE FOR RESIDUE BIP D 311 source : AC8 43) chain D residue 243 type sequence I description BINDING SITE FOR RESIDUE BIP D 311 source : AC8 44) chain D residue 248 type sequence Y description BINDING SITE FOR RESIDUE BIP D 311 source : AC8 45) chain D residue 268 type sequence T description BINDING SITE FOR RESIDUE BIP D 311 source : AC8 46) chain D residue 270 type sequence E description BINDING SITE FOR RESIDUE BIP D 311 source : AC8 47) chain A residue 69 type catalytic sequence H description 171 source MCSA : MCSA1 48) chain A residue 72 type catalytic sequence E description 171 source MCSA : MCSA1 49) chain A residue 127 type catalytic sequence R description 171 source MCSA : MCSA1 50) chain A residue 196 type catalytic sequence H description 171 source MCSA : MCSA1 51) chain A residue 270 type catalytic sequence E description 171 source MCSA : MCSA1 52) chain B residue 69 type catalytic sequence H description 171 source MCSA : MCSA2 53) chain B residue 72 type catalytic sequence E description 171 source MCSA : MCSA2 54) chain B residue 127 type catalytic sequence R description 171 source MCSA : MCSA2 55) chain B residue 196 type catalytic sequence H description 171 source MCSA : MCSA2 56) chain B residue 270 type catalytic sequence E description 171 source MCSA : MCSA2 57) chain C residue 69 type catalytic sequence H description 171 source MCSA : MCSA3 58) chain C residue 72 type catalytic sequence E description 171 source MCSA : MCSA3 59) chain C residue 127 type catalytic sequence R description 171 source MCSA : MCSA3 60) chain C residue 196 type catalytic sequence H description 171 source MCSA : MCSA3 61) chain C residue 270 type catalytic sequence E description 171 source MCSA : MCSA3 62) chain D residue 69 type catalytic sequence H description 171 source MCSA : MCSA4 63) chain D residue 72 type catalytic sequence E description 171 source MCSA : MCSA4 64) chain D residue 127 type catalytic sequence R description 171 source MCSA : MCSA4 65) chain D residue 196 type catalytic sequence H description 171 source MCSA : MCSA4 66) chain D residue 270 type catalytic sequence E description 171 source MCSA : MCSA4 67) chain A residue 60-82 type prosite sequence PAIWIDLGIHSREWITQATGVWF description CARBOXYPEPT_ZN_1 Zinc carboxypeptidases, zinc-binding region 1 signature. PaIwIdlGiHSrEwITQatgvwF source prosite : PS00132 68) chain A residue 196-206 type prosite sequence HSYSQLLLYPY description CARBOXYPEPT_ZN_2 Zinc carboxypeptidases, zinc-binding region 2 signature. HSYSQLLlYPY source prosite : PS00133 69) chain A residue 270 type ACT_SITE sequence E description Proton donor/acceptor => ECO:0000255|PROSITE-ProRule:PRU01379 source Swiss-Prot : SWS_FT_FI1 70) chain B residue 270 type ACT_SITE sequence E description Proton donor/acceptor => ECO:0000255|PROSITE-ProRule:PRU01379 source Swiss-Prot : SWS_FT_FI1 71) chain C residue 270 type ACT_SITE sequence E description Proton donor/acceptor => ECO:0000255|PROSITE-ProRule:PRU01379 source Swiss-Prot : SWS_FT_FI1 72) chain D residue 270 type ACT_SITE sequence E description Proton donor/acceptor => ECO:0000255|PROSITE-ProRule:PRU01379 source Swiss-Prot : SWS_FT_FI1 73) 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 74) chain D 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 75) chain D 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 76) chain D 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 77) 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 78) 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 79) 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 80) 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 81) 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 82) 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 83) 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 84) 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 85) chain A residue 127 type BINDING sequence R description BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 source Swiss-Prot : SWS_FT_FI3 86) chain C residue 144 type BINDING sequence N description BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 source Swiss-Prot : SWS_FT_FI3 87) chain C residue 197 type BINDING sequence S description BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 source Swiss-Prot : SWS_FT_FI3 88) chain C residue 248 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 source Swiss-Prot : SWS_FT_FI3 89) chain D residue 127 type BINDING sequence R description BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 source Swiss-Prot : SWS_FT_FI3 90) chain D residue 144 type BINDING sequence N description BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 source Swiss-Prot : SWS_FT_FI3 91) chain D residue 197 type BINDING sequence S description BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 source Swiss-Prot : SWS_FT_FI3 92) chain D residue 248 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 source Swiss-Prot : SWS_FT_FI3 93) chain A residue 144 type BINDING sequence N description BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 source Swiss-Prot : SWS_FT_FI3 94) chain A residue 197 type BINDING sequence S description BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 source Swiss-Prot : SWS_FT_FI3 95) chain A residue 248 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 source Swiss-Prot : SWS_FT_FI3 96) chain B residue 127 type BINDING sequence R description BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 source Swiss-Prot : SWS_FT_FI3 97) chain B residue 144 type BINDING sequence N description BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 source Swiss-Prot : SWS_FT_FI3 98) chain B residue 197 type BINDING sequence S description BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 source Swiss-Prot : SWS_FT_FI3 99) chain B residue 248 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 source Swiss-Prot : SWS_FT_FI3 100) chain C residue 127 type BINDING sequence R description BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 source Swiss-Prot : SWS_FT_FI3

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