eF-site ID 1js0-A PDB Code 1js0 Chain A click to enlarge Title Crystal Structure of 3D Domain-swapped RNase A Minor Trimer Classification HYDROLASE Compound RIBONUCLEASE A Source ORGANISM_COMMON: cattle; ORGANISM_SCIENTIFIC: Bos taurus; Sequence A:  KETAAAKFERQHMDSSTSAASSSNYCNQMMKSRNLTKDRC KPVNTFVHESLADVQAVCSQKNVACKNGQTNCYQSYSTMS ITDCRETGSSKYPNCAYKTTQANKHIIVACEGNPYVPVHF DASV Description Functional site 1) chain A residue 11 type sequence Q description BINDING SITE FOR RESIDUE SO4 B 602 source : AC2 2) chain A residue 12 type sequence H description BINDING SITE FOR RESIDUE SO4 B 602 source : AC2 3) chain A residue 41 type sequence K description BINDING SITE FOR RESIDUE SO4 B 602 source : AC2 4) chain A residue 118 type sequence V description BINDING SITE FOR RESIDUE SO4 A 603 source : AC3 5) chain A residue 119 type sequence H description BINDING SITE FOR RESIDUE SO4 A 603 source : AC3 6) chain A residue 120 type sequence F description BINDING SITE FOR RESIDUE SO4 A 603 source : AC3 7) chain A residue 111 type sequence E description BINDING SITE FOR RESIDUE SO4 A 604 source : AC4 8) chain A residue 112 type sequence G description BINDING SITE FOR RESIDUE SO4 A 604 source : AC4 9) chain A residue 115 type sequence Y description BINDING SITE FOR RESIDUE SO4 A 604 source : AC4 10) chain A residue 12 type catalytic sequence H description 164 source MCSA : MCSA1 11) chain A residue 41 type catalytic sequence K description 164 source MCSA : MCSA1 12) chain A residue 119 type catalytic sequence H description 164 source MCSA : MCSA1 13) chain A residue 120 type catalytic sequence F description 164 source MCSA : MCSA1 14) chain A residue 121 type catalytic sequence D description 164 source MCSA : MCSA1 15) chain A residue 40-46 type prosite sequence CKPVNTF description RNASE_PANCREATIC Pancreatic ribonuclease family signature. CKpvNTF source prosite : PS00127 16) chain A residue 12 type ACT_SITE sequence H description Proton acceptor source Swiss-Prot : SWS_FT_FI1 17) chain A residue 119 type ACT_SITE sequence H description Proton donor source Swiss-Prot : SWS_FT_FI2 18) chain A residue 7 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 19) chain A residue 10 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI3 20) chain A residue 41 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 21) chain A residue 66 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 22) chain A residue 85 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI3 23) chain A residue 1 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:4030761 source Swiss-Prot : SWS_FT_FI4 24) chain A residue 7 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:4030761 source Swiss-Prot : SWS_FT_FI4 25) chain A residue 37 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:4030761 source Swiss-Prot : SWS_FT_FI4 26) chain A residue 41 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:4030761 source Swiss-Prot : SWS_FT_FI4 27) chain A residue 34 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine; partial => ECO:0000269|PubMed:19358553 source Swiss-Prot : SWS_FT_FI5

Display surface Download Links