eF-site ID 1rtu-A PDB Code 1rtu Chain A click to enlarge Title USTILAGO SPHAEROGENA RIBONUCLEASE U2 Classification HYDROLASE Compound RIBONUCLEASE U2 Source ORGANISM_SCIENTIFIC: Ustilago sphaerogena; Sequence A:  CDIPQSTNCGGNVYSNDDINTAIQGALDDVANGDRPDNYP HQYYXEASEDITLCCGSGPWSEFPLVYNGPYYSSRDNYVS PGPDRVIYQTNTGEFCATVTHTGAASYDGFTQCS Description Functional site 1) chain A residue 39 type sequence Y description CATALYTIC SITE. source : CAT 2) chain A residue 41 type sequence H description CATALYTIC SITE. source : CAT 3) chain A residue 62 type sequence E description CATALYTIC SITE. source : CAT 4) chain A residue 85 type sequence R description CATALYTIC SITE. source : CAT 5) chain A residue 101 type sequence H description CATALYTIC SITE. source : CAT 6) chain A residue 39 type sequence Y description BINDING SITE FOR RESIDUE SO4 A 201 source : AC1 7) chain A residue 41 type sequence H description BINDING SITE FOR RESIDUE SO4 A 201 source : AC1 8) chain A residue 62 type sequence E description BINDING SITE FOR RESIDUE SO4 A 201 source : AC1 9) chain A residue 85 type sequence R description BINDING SITE FOR RESIDUE SO4 A 201 source : AC1 10) chain A residue 101 type sequence H description BINDING SITE FOR RESIDUE SO4 A 201 source : AC1 11) chain A residue 110 type sequence F description BINDING SITE FOR RESIDUE SO4 A 201 source : AC1 12) chain A residue 41 type catalytic sequence H description 908 source MCSA : MCSA1 13) chain A residue 62 type catalytic sequence E description 908 source MCSA : MCSA1 14) chain A residue 85 type catalytic sequence R description 908 source MCSA : MCSA1 15) chain A residue 101 type catalytic sequence H description 908 source MCSA : MCSA1 16) chain A residue 41 type ACT_SITE sequence H description ACT_SITE => ECO:0000269|Ref.5 source Swiss-Prot : SWS_FT_FI1 17) chain A residue 62 type ACT_SITE sequence E description Proton acceptor => ECO:0000269|Ref.5 source Swiss-Prot : SWS_FT_FI2 18) chain A residue 101 type ACT_SITE sequence H description Proton donor => ECO:0000269|Ref.5 source Swiss-Prot : SWS_FT_FI3 19) chain A residue 29 type BINDING sequence D description BINDING => ECO:0000269|PubMed:20858208 source Swiss-Prot : SWS_FT_FI4 20) chain A residue 30 type BINDING sequence V description BINDING => ECO:0000269|PubMed:20858208 source Swiss-Prot : SWS_FT_FI4 21) chain A residue 31 type BINDING sequence A description BINDING => ECO:0000269|PubMed:20858208 source Swiss-Prot : SWS_FT_FI4 22) chain A residue 32 type BINDING sequence N description BINDING => ECO:0000269|PubMed:20858208 source Swiss-Prot : SWS_FT_FI4 23) chain A residue 37 type BINDING sequence D description BINDING => ECO:0000269|PubMed:20858208 source Swiss-Prot : SWS_FT_FI4 24) chain A residue 39 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:20858208 source Swiss-Prot : SWS_FT_FI4 25) chain A residue 85 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI5 26) chain A residue 108 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI5 27) chain A residue 62 type SITE sequence E description Methylation inactivates enzyme => ECO:0000269|PubMed:7492561 source Swiss-Prot : SWS_FT_FI6

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