eF-site ID 1u20-AB PDB Code 1u20 Chain A, B click to enlarge Title Crystal Structure of Xenopus laevis nudix hydrolase nuclear SnoRNA decapping Protein X29 Classification HYDROLASE Compound U8 snoRNA-binding protein X29 Source Xenopus laevis (African clawed frog) (Q6TEC1_XENLA) Sequence A:  DKPRPRNISREESLQLEGYKHACHALLHAPSQAKLFDRVP IRRVLLMMMRFDGRLGFPGGFVDTRDISLEEGLKRELEEE LGPALATVEVTEDDYRSSQVREHPQKCVTHFYIKELKLEE IERIEAEAVNAKDHGLEVMGLIRVPLYTLRDRVGGLPAFL CNNFIGNSKSQLLYALRSLKLLREDQIQEVLKASHR B:  PRNISREESLQLEGYKHACHALLHAPSQAKLFDRVPIRRV LLMMMRFDGRLGFPGGFVDTRDISLEEGLKRELEEELGPA LATVEVTEDDYRSSQVREHPQKCVTHFYIKELKLEEIERI EAEAVNAKDHGLEVMGLIRVPLYTLRDRVGGLPAFLCNNF IGNSKSQLLYALRSLKLLREDQIQEVLKASHR Description Functional site 1) chain A residue 132 type sequence E description BINDING SITE FOR RESIDUE GOL A 500 source : AC1 2) chain A residue 135 type sequence E description BINDING SITE FOR RESIDUE GOL A 500 source : AC1 3) chain A residue 163 type sequence R description BINDING SITE FOR RESIDUE GOL A 500 source : AC1 4) chain B residue 37 type sequence H description BINDING SITE FOR RESIDUE GOL B 501 source : AC2 5) chain B residue 63 type sequence R description BINDING SITE FOR RESIDUE GOL B 501 source : AC2 6) chain A residue 37 type BINDING sequence H description BINDING => ECO:0000269|PubMed:16472752 source Swiss-Prot : SWS_FT_FI1 7) chain B residue 63 type BINDING sequence R description BINDING => ECO:0000269|PubMed:16472752 source Swiss-Prot : SWS_FT_FI1 8) chain B residue 72 type BINDING sequence G description BINDING => ECO:0000269|PubMed:16472752 source Swiss-Prot : SWS_FT_FI1 9) chain B residue 89 type BINDING sequence E description BINDING => ECO:0000269|PubMed:16472752 source Swiss-Prot : SWS_FT_FI1 10) chain B residue 93 type BINDING sequence E description BINDING => ECO:0000269|PubMed:16472752 source Swiss-Prot : SWS_FT_FI1 11) chain B residue 150 type BINDING sequence E description BINDING => ECO:0000269|PubMed:16472752 source Swiss-Prot : SWS_FT_FI1 12) chain B residue 180 type BINDING sequence N description BINDING => ECO:0000269|PubMed:16472752 source Swiss-Prot : SWS_FT_FI1 13) chain B residue 184 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:16472752 source Swiss-Prot : SWS_FT_FI1 14) chain A residue 63 type BINDING sequence R description BINDING => ECO:0000269|PubMed:16472752 source Swiss-Prot : SWS_FT_FI1 15) chain A residue 72 type BINDING sequence G description BINDING => ECO:0000269|PubMed:16472752 source Swiss-Prot : SWS_FT_FI1 16) chain A residue 89 type BINDING sequence E description BINDING => ECO:0000269|PubMed:16472752 source Swiss-Prot : SWS_FT_FI1 17) chain A residue 93 type BINDING sequence E description BINDING => ECO:0000269|PubMed:16472752 source Swiss-Prot : SWS_FT_FI1 18) chain A residue 150 type BINDING sequence E description BINDING => ECO:0000269|PubMed:16472752 source Swiss-Prot : SWS_FT_FI1 19) chain A residue 180 type BINDING sequence N description BINDING => ECO:0000269|PubMed:16472752 source Swiss-Prot : SWS_FT_FI1 20) chain A residue 184 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:16472752 source Swiss-Prot : SWS_FT_FI1 21) chain B residue 37 type BINDING sequence H description BINDING => ECO:0000269|PubMed:16472752 source Swiss-Prot : SWS_FT_FI1 22) chain A residue 70 type BINDING sequence F description BINDING => ECO:0000250|UniProtKB:Q96DE0 source Swiss-Prot : SWS_FT_FI2 23) chain B residue 70 type BINDING sequence F description BINDING => ECO:0000250|UniProtKB:Q96DE0 source Swiss-Prot : SWS_FT_FI2

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