eF-site ID 5w6x-AB PDB Code 5w6x Chain A, B click to enlarge Title Crystal structure of the HsNUDT16 in complex with Mg+2 and ADP-ribose Classification HYDROLASE Compound U8 snoRNA-decapping enzyme Source (NUD16_HUMAN) Sequence A:  GARRLELGEALALGSGWRHVCHALLYAPDPGMLFGRIPLR YAILMQMRFDGRLGFPGGFVDTQDRSLEDGLNRELREELG EAAAAFRVERTDYRSSHVGSGPRVVAHFYAKRLTLEELLA VEAGATRAKDHGLEVLGLVRVPLYTLRDGVGGLPTFLENS FIGSAREQLLEALQDLGLL B:  ARRLELGEALALGSGWRHVCHALLYAPDPGMLFGRIPLRY AILMQMRFDGRLGFPGGFVDQDRSLEDGLNRELREELGEA AAAFRVERTDYRSSHVPRVVAHFYAKRLTLEELLAVEAGA TRAKDHGLEVLGLVRVPLYTLRDGVGGLPTFLENSFIGSA REQLLEALQDLGLL Description Functional site 1) chain A residue 22 type sequence V description binding site for residue APR A 401 source : AC1 2) chain A residue 24 type sequence H description binding site for residue APR A 401 source : AC1 3) chain A residue 50 type sequence R description binding site for residue APR A 401 source : AC1 4) chain A residue 59 type sequence G description binding site for residue APR A 401 source : AC1 5) chain A residue 60 type sequence G description binding site for residue APR A 401 source : AC1 6) chain A residue 61 type sequence F description binding site for residue APR A 401 source : AC1 7) chain A residue 76 type sequence E description binding site for residue APR A 401 source : AC1 8) chain A residue 80 type sequence E description binding site for residue APR A 401 source : AC1 9) chain A residue 108 type sequence A description binding site for residue APR A 401 source : AC1 10) chain A residue 136 type sequence E description binding site for residue APR A 401 source : AC1 11) chain A residue 164 type sequence I description binding site for residue APR A 401 source : AC1 12) chain A residue 166 type sequence S description binding site for residue APR A 401 source : AC1 13) chain A residue 167 type sequence A description binding site for residue APR A 401 source : AC1 14) chain A residue 170 type sequence Q description binding site for residue APR A 401 source : AC1 15) chain B residue 36 type sequence F description binding site for residue APR A 401 source : AC1 16) chain A residue 76 type sequence E description binding site for residue MG A 402 source : AC2 17) chain A residue 80 type sequence E description binding site for residue MG A 402 source : AC2 18) chain A residue 136 type sequence E description binding site for residue MG A 402 source : AC2 19) chain A residue 59 type sequence G description binding site for residue MG A 403 source : AC3 20) chain A residue 80 type sequence E description binding site for residue MG A 403 source : AC3 21) chain A residue 13 type sequence L description binding site for residue ACY A 404 source : AC4 22) chain B residue 24 type sequence H description binding site for residue APR B 401 source : AC5 23) chain B residue 50 type sequence R description binding site for residue APR B 401 source : AC5 24) chain B residue 51 type sequence F description binding site for residue APR B 401 source : AC5 25) chain B residue 60 type sequence G description binding site for residue APR B 401 source : AC5 26) chain B residue 61 type sequence F description binding site for residue APR B 401 source : AC5 27) chain B residue 76 type sequence E description binding site for residue APR B 401 source : AC5 28) chain B residue 80 type sequence E description binding site for residue APR B 401 source : AC5 29) chain B residue 108 type sequence A description binding site for residue APR B 401 source : AC5 30) chain B residue 136 type sequence E description binding site for residue APR B 401 source : AC5 31) chain B residue 164 type sequence I description binding site for residue APR B 401 source : AC5 32) chain B residue 166 type sequence S description binding site for residue APR B 401 source : AC5 33) chain B residue 170 type sequence Q description binding site for residue APR B 401 source : AC5 34) chain B residue 76 type sequence E description binding site for residue MG B 402 source : AC6 35) chain B residue 80 type sequence E description binding site for residue MG B 402 source : AC6 36) chain B residue 132 type sequence D description binding site for residue MG B 402 source : AC6 37) chain B residue 136 type sequence E description binding site for residue MG B 402 source : AC6 38) chain B residue 59 type sequence G description binding site for residue MG B 403 source : AC7 39) chain B residue 80 type sequence E description binding site for residue MG B 403 source : AC7 40) chain B residue 82 type sequence G description binding site for residue ACY B 404 source : AC8 41) chain B residue 83 type sequence E description binding site for residue ACY B 404 source : AC8 42) chain B residue 84 type sequence A description binding site for residue ACY B 404 source : AC8 43) chain B residue 126 type sequence G description binding site for residue ACY B 404 source : AC8 44) chain B residue 129 type sequence R description binding site for residue ACY B 404 source : AC8 45) chain B residue 30 type sequence P description binding site for residue PEG B 405 source : AC9 46) chain B residue 114 type sequence R description binding site for residue PEG B 405 source : AC9 47) chain B residue 115 type sequence L description binding site for residue PEG B 405 source : AC9 48) chain B residue 116 type sequence T description binding site for residue PEG B 405 source : AC9 49) chain B residue 117 type sequence L description binding site for residue PEG B 405 source : AC9 50) chain A residue 59 type BINDING sequence G description BINDING => ECO:0000269|PubMed:32432673, ECO:0000305|PubMed:26121039, ECO:0007744|PDB:6X7U source Swiss-Prot : SWS_FT_FI2 51) chain B residue 59 type BINDING sequence G description BINDING => ECO:0000269|PubMed:32432673, ECO:0000305|PubMed:26121039, ECO:0007744|PDB:6X7U source Swiss-Prot : SWS_FT_FI2 52) chain A residue 24 type BINDING sequence H description BINDING => ECO:0000305|PubMed:26121039 source Swiss-Prot : SWS_FT_FI1 53) chain A residue 50 type BINDING sequence R description BINDING => ECO:0000305|PubMed:26121039 source Swiss-Prot : SWS_FT_FI1 54) chain A residue 57 type BINDING sequence F description BINDING => ECO:0000305|PubMed:26121039 source Swiss-Prot : SWS_FT_FI1 55) chain A residue 170 type BINDING sequence Q description BINDING => ECO:0000305|PubMed:26121039 source Swiss-Prot : SWS_FT_FI1 56) chain B residue 24 type BINDING sequence H description BINDING => ECO:0000305|PubMed:26121039 source Swiss-Prot : SWS_FT_FI1 57) chain B residue 50 type BINDING sequence R description BINDING => ECO:0000305|PubMed:26121039 source Swiss-Prot : SWS_FT_FI1 58) chain B residue 57 type BINDING sequence F description BINDING => ECO:0000305|PubMed:26121039 source Swiss-Prot : SWS_FT_FI1 59) chain B residue 170 type BINDING sequence Q description BINDING => ECO:0000305|PubMed:26121039 source Swiss-Prot : SWS_FT_FI1 60) chain A residue 76 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:Q6TEC1 source Swiss-Prot : SWS_FT_FI3 61) chain A residue 80 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:Q6TEC1 source Swiss-Prot : SWS_FT_FI3 62) chain B residue 76 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:Q6TEC1 source Swiss-Prot : SWS_FT_FI3 63) chain B residue 80 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:Q6TEC1 source Swiss-Prot : SWS_FT_FI3 64) chain A residue 99 type BINDING sequence H description BINDING => ECO:0000269|PubMed:32432673, ECO:0007744|PDB:6X7U, ECO:0007744|PDB:6X7V source Swiss-Prot : SWS_FT_FI4 65) chain A residue 173 type BINDING sequence E description BINDING => ECO:0000269|PubMed:32432673, ECO:0007744|PDB:6X7U, ECO:0007744|PDB:6X7V source Swiss-Prot : SWS_FT_FI4 66) chain B residue 99 type BINDING sequence H description BINDING => ECO:0000269|PubMed:32432673, ECO:0007744|PDB:6X7U, ECO:0007744|PDB:6X7V source Swiss-Prot : SWS_FT_FI4 67) chain B residue 173 type BINDING sequence E description BINDING => ECO:0000269|PubMed:32432673, ECO:0007744|PDB:6X7U, ECO:0007744|PDB:6X7V source Swiss-Prot : SWS_FT_FI4

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