eF-site ID 5qji-D PDB Code 5qji Chain D click to enlarge Title PanDDA analysis group deposition of models with modelled events (e.g. bound ligands) -- Crystal Structure of NUDT5 in complex with Z1899842917 Classification HYDROLASE Compound ADP-sugar pyrophosphatase Source (NUDT5_HUMAN) Sequence D:  KQYIISEELISEGKWVKLEKTTYMDPTGKTRTWESVKRTT ADGVAVIPVLQRTLHYECIVLVKQFRPPMGGYCIEFPAGL IDDGETPEAAALRELEEETGYKGDIAECSPAVCMDPGLSN CTIHIVTVTINGDDAENARPKPKPGDGEFVEVISLPKNDL LQRLDALVAEEHLTVDARVYSYALALKHAN Description Functional site 1) chain D residue 82 type sequence Q description binding site for residue MG D 301 source : AD2 2) chain D residue 84 type sequence R description binding site for residue MG D 301 source : AD2 3) chain D residue 96 type sequence A description binding site for residue MG D 301 source : AD2 4) chain D residue 116 type sequence E description binding site for residue MG D 301 source : AD2 5) chain D residue 166 type sequence E description binding site for residue MG D 301 source : AD2 6) chain D residue 96 type sequence A description binding site for residue MG D 302 source : AD3 7) chain D residue 112 type sequence E description binding site for residue MG D 302 source : AD3 8) chain D residue 116 type sequence E description binding site for residue MG D 302 source : AD3 9) chain D residue 166 type sequence E description binding site for residue MG D 302 source : AD3 10) chain D residue 46 type sequence W description binding site for residue K1A D 303 source : AD4 11) chain D residue 47 type sequence E description binding site for residue K1A D 303 source : AD4 12) chain D residue 135 type sequence G description binding site for residue K1A D 303 source : AD4 13) chain D 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 14) chain D 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 15) chain D 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 16) chain D 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 17) chain D 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 18) chain D 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 19) chain D 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 20) chain D 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 21) chain D 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 22) chain D residue 98 type BINDING sequence L description in other chain => ECO:0000269|PubMed:17052728 source Swiss-Prot : SWS_FT_FI3 23) chain D residue 133 type BINDING sequence D description in other chain => ECO:0000269|PubMed:17052728 source Swiss-Prot : SWS_FT_FI3 24) chain D residue 45 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:27257257 source Swiss-Prot : SWS_FT_FI7 25) chain D residue 74 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI8

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