eF-site ID 5qj6-C PDB Code 5qj6 Chain C click to enlarge Title PanDDA analysis group deposition of models with modelled events (e.g. bound ligands) -- Crystal Structure of NUDT5 in complex with Z1614545742 Classification HYDROLASE Compound ADP-sugar pyrophosphatase Source (NUDT5_HUMAN) Sequence C:  QYIISEELISEGKWVKLEKTTYMDPTGKTRTWESVKRTTR KQTADGVAVIPVLQRTLHYECIVLVKQFRPPMGGYCIEFP AGLIDDGETPEAAALRELEEETGYKGDIAECSPAVCMDPG LSNCTIHIVTVTINGDDAENARPKPKPGDGEFVEVISLPK NDLLQRLDALVAEEHLTVDARVYSYALALKHA Description Functional site 1) chain C residue 122 type sequence D description binding site for residue EDO C 301 source : AC9 2) chain C residue 152 type sequence D description binding site for residue EDO C 301 source : AC9 3) chain C residue 154 type sequence E description binding site for residue EDO C 301 source : AC9 4) chain C residue 155 type sequence N description binding site for residue EDO C 301 source : AC9 5) chain C residue 96 type sequence A description binding site for residue MG C 302 source : AD1 6) chain C residue 112 type sequence E description binding site for residue MG C 302 source : AD1 7) chain C residue 116 type sequence E description binding site for residue MG C 302 source : AD1 8) chain C residue 166 type sequence E description binding site for residue MG C 302 source : AD1 9) chain C residue 96 type sequence A description binding site for residue MG C 303 source : AD2 10) chain C residue 116 type sequence E description binding site for residue MG C 303 source : AD2 11) chain C residue 166 type sequence E description binding site for residue MG C 303 source : AD2 12) chain C residue 51 type sequence R description binding site for residue EDO C 304 source : AD3 13) chain C residue 139 type sequence C description binding site for residue EDO C 304 source : AD3 14) chain C residue 206 type sequence H description binding site for residue GQJ D 303 source : AD6 15) chain C residue 133 type sequence D description binding site for residue EDO D 304 source : AD7 16) chain C residue 45 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:27257257 source Swiss-Prot : SWS_FT_FI7 17) chain C residue 74 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI8 18) chain C residue 42 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI9 19) chain C residue 28 type BINDING sequence W description in other chain => ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126 source Swiss-Prot : SWS_FT_FI1 20) chain C residue 84 type BINDING sequence R description in other chain => ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126 source Swiss-Prot : SWS_FT_FI1 21) chain C residue 46 type BINDING sequence W description BINDING => ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126 source Swiss-Prot : SWS_FT_FI2 22) chain C residue 51 type BINDING sequence R description BINDING => ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126 source Swiss-Prot : SWS_FT_FI2 23) chain C residue 96 type BINDING sequence A description BINDING => ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126 source Swiss-Prot : SWS_FT_FI2 24) chain C residue 112 type BINDING sequence E description BINDING => ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126 source Swiss-Prot : SWS_FT_FI2 25) chain C residue 116 type BINDING sequence E description BINDING => ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126 source Swiss-Prot : SWS_FT_FI2 26) chain C residue 166 type BINDING sequence E description BINDING => ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126 source Swiss-Prot : SWS_FT_FI2 27) chain C residue 98 type BINDING sequence L description in other chain => ECO:0000269|PubMed:17052728 source Swiss-Prot : SWS_FT_FI3 28) chain C residue 133 type BINDING sequence D description in other chain => ECO:0000269|PubMed:17052728 source Swiss-Prot : SWS_FT_FI3

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