eF-site ID 1dyt-AB PDB Code 1dyt Chain A, B click to enlarge Title X-ray crystal structure of ECP (RNase 3) at 1.75 A Classification HYDROLASE Compound EOSINOPHIL CATIONIC PROTEIN Source Homo sapiens (Human) (ECP_HUMAN) Sequence A:  RPPQFTRAQWFAIQHISLNPPRCTIAMRAINNYRWRCKNQ NTFLRTTFANVVNVCGNQSIRCPHNRTLNNCHRSRFRVPL LHCDLINPGAQNISNCRYADRPGRRFYVVACDNRDPRDSP RYPVVPVHLDTTI B:  RPPQFTRAQWFAIQHISLNPPRCTIAMRAINNYRWRCKNQ NTFLRTTFANVVNVCGNQSIRCPHNRTLNNCHRSRFRVPL LHCDLINPGAQNISNCRYADRPGRRFYVVACDNRDPRDSP RYPVVPVHLDTTI Description (1)  EOSINOPHIL CATIONIC PROTEIN (E.C.3.1.27.-) Functional site 1) chain B residue 34 type sequence R description BINDING SITE FOR RESIDUE FE B 300 source : AC1 2) chain A residue 46 type sequence T description BINDING SITE FOR RESIDUE CIT A 301 source : AC3 3) chain A residue 50 type sequence N description BINDING SITE FOR RESIDUE CIT A 301 source : AC3 4) chain A residue 54 type sequence V description BINDING SITE FOR RESIDUE CIT A 301 source : AC3 5) chain A residue 74 type sequence S description BINDING SITE FOR RESIDUE CIT A 301 source : AC3 6) chain A residue 75 type sequence R description BINDING SITE FOR RESIDUE CIT A 301 source : AC3 7) chain A residue 76 type sequence F description BINDING SITE FOR RESIDUE CIT A 301 source : AC3 8) chain A residue 78 type sequence V description BINDING SITE FOR RESIDUE CIT A 301 source : AC3 9) chain A residue 107 type sequence Y description BINDING SITE FOR RESIDUE CIT A 301 source : AC3 10) chain B residue 121 type sequence R description BINDING SITE FOR RESIDUE CIT A 301 source : AC3 11) chain A residue 61 type sequence R description BINDING SITE FOR RESIDUE CIT B 301 source : AC4 12) chain A residue 66 type sequence R description BINDING SITE FOR RESIDUE CIT B 301 source : AC4 13) chain B residue 46 type sequence T description BINDING SITE FOR RESIDUE CIT B 301 source : AC4 14) chain B residue 50 type sequence N description BINDING SITE FOR RESIDUE CIT B 301 source : AC4 15) chain B residue 54 type sequence V description BINDING SITE FOR RESIDUE CIT B 301 source : AC4 16) chain B residue 74 type sequence S description BINDING SITE FOR RESIDUE CIT B 301 source : AC4 17) chain B residue 75 type sequence R description BINDING SITE FOR RESIDUE CIT B 301 source : AC4 18) chain B residue 76 type sequence F description BINDING SITE FOR RESIDUE CIT B 301 source : AC4 19) chain B residue 78 type sequence V description BINDING SITE FOR RESIDUE CIT B 301 source : AC4 20) chain B residue 107 type sequence Y description BINDING SITE FOR RESIDUE CIT B 301 source : AC4 21) chain A residue 34 type sequence R description BINDING SITE FOR RESIDUE CIT A 302 source : AC5 22) chain A residue 38 type sequence K description BINDING SITE FOR RESIDUE CIT A 302 source : AC5 23) chain A residue 39 type sequence N description BINDING SITE FOR RESIDUE CIT A 302 source : AC5 24) chain A residue 40 type sequence Q description BINDING SITE FOR RESIDUE CIT A 302 source : AC5 25) chain B residue 34 type sequence R description BINDING SITE FOR RESIDUE CIT B 302 source : AC6 26) chain B residue 36 type sequence R description BINDING SITE FOR RESIDUE CIT B 302 source : AC6 27) chain B residue 37 type sequence C description BINDING SITE FOR RESIDUE CIT B 302 source : AC6 28) chain B residue 38 type sequence K description BINDING SITE FOR RESIDUE CIT B 302 source : AC6 29) chain B residue 39 type sequence N description BINDING SITE FOR RESIDUE CIT B 302 source : AC6 30) chain B residue 40 type sequence Q description BINDING SITE FOR RESIDUE CIT B 302 source : AC6 31) chain A residue 38 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 32) chain B residue 38 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 33) chain A residue 33 type SITE sequence Y description May be involved in LPS-binding source Swiss-Prot : SWS_FT_FI4 34) chain B residue 33 type SITE sequence Y description May be involved in LPS-binding source Swiss-Prot : SWS_FT_FI4 35) chain A residue 15 type ACT_SITE sequence H description Proton acceptor source Swiss-Prot : SWS_FT_FI1 36) chain B residue 15 type ACT_SITE sequence H description Proton acceptor source Swiss-Prot : SWS_FT_FI1 37) chain A residue 128 type ACT_SITE sequence H description Proton donor source Swiss-Prot : SWS_FT_FI2 38) chain B residue 128 type ACT_SITE sequence H description Proton donor source Swiss-Prot : SWS_FT_FI2 39) chain A residue 57 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI7 40) chain A residue 65 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI7 41) chain A residue 92 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI7 42) chain B residue 57 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI7 43) chain B residue 65 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI7 44) chain B residue 92 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI7 45) chain A residue 35 type SITE sequence W description May be involved in LPS- and LTA-binding source Swiss-Prot : SWS_FT_FI5 46) chain B residue 35 type SITE sequence W description May be involved in LPS- and LTA-binding source Swiss-Prot : SWS_FT_FI5 47) chain A residue 33 type MOD_RES sequence Y description 3'-nitrotyrosine => ECO:0000269|PubMed:18694936 source Swiss-Prot : SWS_FT_FI6 48) chain B residue 33 type MOD_RES sequence Y description 3'-nitrotyrosine => ECO:0000269|PubMed:18694936 source Swiss-Prot : SWS_FT_FI6 49) chain A residue 37-43 type prosite sequence CKNQNTF description RNASE_PANCREATIC Pancreatic ribonuclease family signature. CKnqNTF source prosite : PS00127

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