eF-site ID 1jl2-ABCD PDB Code 1jl2 Chain A, B, C, D click to enlarge Title Crystal structure of TCEO RNase H-a chimera combining the folding core from T. thermophilus RNase H and the remaining region of E. coli RNase H Classification HYDROLASE Compound Chimera of Ribonuclease HI, Ribonuclease H Source Escherichia coli (strain K12) (RNH_ECOLI) Sequence A:  KQVEIFTDGSALGNPGPGGYGAILRYRGREKTFSAGYTRT TNNRMELKAAIEGLKALKEPAEVDLYTDSHYLKKAFTEGW LEGWRKRGWRTAEGKPVKNRDLWEALLLAMAPHRVRFHFV KGHAGHPENERADELARAAAMNPTLEDTGY B:  KQVEIFTDGSALGNPGPGGYGAILRYRGREKTFSAGYTRT TNNRMELKAAIEGLKALKEPAEVDLYTDSHYLKKAFTEPV KNRDLWEALLLAMAPHRVRFHFVKGHAGHPENERADELAR AAAMNPTLEDTGY C:  KQVEIFTDGSALGNPGPGGYGAILRYRGREKTFSAGYTRT TNNRMELKAAIEGLKALKEPAEVDLYTDSHYLKKAFTEVK NRDLWEALLLAMAPHRVRFHFVKGHAGHPENERADELARA AAMNPTLEDTGYQ D:  KQVEIFTDGSALGNPGPGGYGAILRYRGREKTFSAGYTRT TNNRMELKAAIEGLKALKEPAEVDLYTDSHYLKKAFTEGW LEGWRTAEGKPVKNRDLWEALLLAMAPHRVRFHFVKGHAG HPENERADELARAAAMNPTLEDTGYQ Description Functional site 1) chain A residue 10 type catalytic sequence D description 163 source MCSA : MCSA1 2) chain A residue 11 type catalytic sequence G description 163 source MCSA : MCSA1 3) chain A residue 48 type catalytic sequence E description 163 source MCSA : MCSA1 4) chain A residue 125 type catalytic sequence H description 163 source MCSA : MCSA1 5) chain A residue 135 type catalytic sequence D description 163 source MCSA : MCSA1 6) chain B residue 10 type catalytic sequence D description 163 source MCSA : MCSA2 7) chain B residue 11 type catalytic sequence G description 163 source MCSA : MCSA2 8) chain B residue 48 type catalytic sequence E description 163 source MCSA : MCSA2 9) chain B residue 125 type catalytic sequence H description 163 source MCSA : MCSA2 10) chain B residue 135 type catalytic sequence D description 163 source MCSA : MCSA2 11) chain C residue 10 type catalytic sequence D description 163 source MCSA : MCSA3 12) chain C residue 11 type catalytic sequence G description 163 source MCSA : MCSA3 13) chain C residue 48 type catalytic sequence E description 163 source MCSA : MCSA3 14) chain C residue 125 type catalytic sequence H description 163 source MCSA : MCSA3 15) chain C residue 135 type catalytic sequence D description 163 source MCSA : MCSA3 16) chain D residue 10 type catalytic sequence D description 163 source MCSA : MCSA4 17) chain D residue 11 type catalytic sequence G description 163 source MCSA : MCSA4 18) chain D residue 48 type catalytic sequence E description 163 source MCSA : MCSA4 19) chain D residue 125 type catalytic sequence H description 163 source MCSA : MCSA4 20) chain D residue 135 type catalytic sequence D description 163 source MCSA : MCSA4 21) chain A residue 48 type BINDING sequence E description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 22) chain B residue 48 type BINDING sequence E description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 23) chain C residue 48 type BINDING sequence E description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 24) chain D residue 48 type BINDING sequence E description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 25) chain A residue 70 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 26) chain B residue 70 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 27) chain C residue 70 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 28) chain D residue 70 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 29) chain A residue 10 type BINDING sequence D description BINDING => ECO:0000269|PubMed:1311386 source Swiss-Prot : SWS_FT_FI1 30) chain A residue 135 type BINDING sequence D description BINDING => ECO:0000269|PubMed:1311386 source Swiss-Prot : SWS_FT_FI1 31) chain B residue 10 type BINDING sequence D description BINDING => ECO:0000269|PubMed:1311386 source Swiss-Prot : SWS_FT_FI1 32) chain B residue 135 type BINDING sequence D description BINDING => ECO:0000269|PubMed:1311386 source Swiss-Prot : SWS_FT_FI1 33) chain C residue 10 type BINDING sequence D description BINDING => ECO:0000269|PubMed:1311386 source Swiss-Prot : SWS_FT_FI1 34) chain C residue 135 type BINDING sequence D description BINDING => ECO:0000269|PubMed:1311386 source Swiss-Prot : SWS_FT_FI1 35) chain D residue 10 type BINDING sequence D description BINDING => ECO:0000269|PubMed:1311386 source Swiss-Prot : SWS_FT_FI1 36) chain D residue 135 type BINDING sequence D description BINDING => ECO:0000269|PubMed:1311386 source Swiss-Prot : SWS_FT_FI1

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