eF-site ID 5qj8-A PDB Code 5qj8 Chain A click to enlarge Title PanDDA analysis group deposition of models with modelled events (e.g. bound ligands) -- Crystal Structure of NUDT5 in complex with Z2856434829 Classification HYDROLASE Compound ADP-sugar pyrophosphatase Source (NUDT5_HUMAN) Sequence A:  KQYIISEELISEGKWVKLEKTTYMDPTGKTRTWESVKRTT RKEQTADGVAVIPVLQRTLHYECIVLVKQFRPPMGGYCIE FPAGLIDDGETPEAAALRELEEETGYKGDIAECSPAVCMD PGLSNCTIHIVTVTINGDDAENARPKPKPGDGEFVEVISL PKNDLLQRLDALVAEEHLTVDARVYSYALALKHA Description Functional site 1) chain A residue 96 type sequence A description binding site for residue MG A 301 source : AC1 2) chain A residue 116 type sequence E description binding site for residue MG A 301 source : AC1 3) chain A residue 112 type sequence E description binding site for residue MG A 302 source : AC2 4) chain A residue 116 type sequence E description binding site for residue MG A 302 source : AC2 5) chain A residue 166 type sequence E description binding site for residue MG A 302 source : AC2 6) chain A residue 28 type sequence W description binding site for residue ELQ B 305 source : AC6 7) chain A residue 51 type sequence R description binding site for residue ELQ B 305 source : AC6 8) chain A residue 97-118 type prosite sequence GLIDDGETPEAAALRELEEETG description NUDIX_BOX Nudix box signature. GliddgEtpeaAAlRELeEEtG source prosite : PS00893 9) chain A 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 10) chain A 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 11) chain A 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 12) chain A 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 13) chain A 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 14) chain A 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 15) chain A 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 16) chain A 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 17) chain A residue 133 type BINDING sequence D description in other chain => ECO:0000269|PubMed:17052728 source Swiss-Prot : SWS_FT_FI3 18) chain A residue 98 type BINDING sequence L description in other chain => ECO:0000269|PubMed:17052728 source Swiss-Prot : SWS_FT_FI3 19) chain A residue 45 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:27257257 source Swiss-Prot : SWS_FT_FI7 20) chain A residue 74 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI8 21) chain A 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

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