eF-site ID 9rsa-B PDB Code 9rsa Chain B click to enlarge Title CRYSTAL STRUCTURE OF TWO COVALENT NUCLEOSIDE DERIVATIVES OF RIBONUCLEASE A Classification HYDROLASE (PHOSPHORIC DIESTER) Compound RIBONUCLEASE A Source Bos taurus (Bovine) (RNAS1_BOVIN) Sequence B:  KETAAAKFERQHMDSSTSAASSSNYCNQMMKSRNLTKDRC KPVNTFVHESLADVQAVCSQKNVACKNGQTNCYQSYSTMS ITDCRETGSSKYPNCAYKTTQANKHIIVACEGNPYVPVHF DASV Description (1)  RIBONUCLEASE A (PHOSPHATE-FREE) (E.C.3.1.27.5) COMPLEX WITH ND1.119-N-ACETYL DEOXYURIDINE Functional site 1) chain B residue 12 type sequence H description ACTIVE SITE OF THE ENZYME IN CHAIN B source : AD2 2) chain B residue 41 type sequence K description ACTIVE SITE OF THE ENZYME IN CHAIN B source : AD2 3) chain B residue 43 type sequence V description ACTIVE SITE OF THE ENZYME IN CHAIN B source : AD2 4) chain B residue 44 type sequence N description ACTIVE SITE OF THE ENZYME IN CHAIN B source : AD2 5) chain B residue 45 type sequence T description ACTIVE SITE OF THE ENZYME IN CHAIN B source : AD2 6) chain B residue 119 type sequence H description ACTIVE SITE OF THE ENZYME IN CHAIN B source : AD2 7) chain B residue 120 type sequence F description ACTIVE SITE OF THE ENZYME IN CHAIN B source : AD2 8) chain B residue 121 type sequence D description ACTIVE SITE OF THE ENZYME IN CHAIN B source : AD2 9) chain B residue 123 type sequence S description ACTIVE SITE OF THE ENZYME IN CHAIN B source : AD2 10) chain B residue 118 type sequence V description BINDING SITE FOR RESIDUE ADU B 125 source : AC2 11) chain B residue 119 type sequence H description BINDING SITE FOR RESIDUE ADU B 125 source : AC2 12) chain B residue 12 type catalytic sequence H description 164 source MCSA : MCSA2 13) chain B residue 41 type catalytic sequence K description 164 source MCSA : MCSA2 14) chain B residue 119 type catalytic sequence H description 164 source MCSA : MCSA2 15) chain B residue 120 type catalytic sequence F description 164 source MCSA : MCSA2 16) chain B residue 121 type catalytic sequence D description 164 source MCSA : MCSA2 17) chain B residue 85 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI3 18) chain B residue 7 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 19) chain B residue 10 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI3 20) chain B residue 41 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 21) chain B residue 66 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 22) chain B residue 1 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:4030761 source Swiss-Prot : SWS_FT_FI4 23) chain B residue 7 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:4030761 source Swiss-Prot : SWS_FT_FI4 24) chain B residue 37 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:4030761 source Swiss-Prot : SWS_FT_FI4 25) chain B residue 41 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:4030761 source Swiss-Prot : SWS_FT_FI4 26) chain B residue 34 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine; partial => ECO:0000269|PubMed:19358553 source Swiss-Prot : SWS_FT_FI5 27) chain B residue 12 type ACT_SITE sequence H description Proton acceptor source Swiss-Prot : SWS_FT_FI1 28) chain B residue 119 type ACT_SITE sequence H description Proton donor source Swiss-Prot : SWS_FT_FI2

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