eF-site ID 5qjj-B PDB Code 5qjj Chain B click to enlarge Title PanDDA analysis group deposition of models with modelled events (e.g. bound ligands) -- Crystal Structure of NUDT5 in complex with Z24758179 Classification HYDROLASE Compound ADP-sugar pyrophosphatase Source (NUDT5_HUMAN) Sequence B:  KQYIISEELISEGKWVKLEKTTYMDPTGKTRTWESVKRTT RKQTADGVAVIPVLQRTLHYECIVLVKQFRPPMGGYCIEF PAGLIDDGETPEAAALRELEEETGYKGDIAECSPAVCMDP GLSNCTIHIVTVTINGDDAENARPKPKPGDGEFVEVISLP KNDLLQRLDALVAEEHLTVDARVYSYALALKHAN Description Functional site 1) chain B residue 133 type sequence D description binding site for residue EDO A 304 source : AC3 2) chain B residue 69 type sequence Q description binding site for residue EDO B 301 source : AC4 3) chain B residue 149 type sequence N description binding site for residue EDO B 301 source : AC4 4) chain B residue 151 type sequence D description binding site for residue EDO B 301 source : AC4 5) chain B residue 96 type sequence A description binding site for residue MG B 302 source : AC5 6) chain B residue 116 type sequence E description binding site for residue MG B 302 source : AC5 7) chain B residue 112 type sequence E description binding site for residue MG B 303 source : AC6 8) chain B residue 115 type sequence E description binding site for residue MG B 303 source : AC6 9) chain B residue 116 type sequence E description binding site for residue MG B 303 source : AC6 10) chain B residue 166 type sequence E description binding site for residue MG B 303 source : AC6 11) chain B residue 51 type sequence R description binding site for residue EDO B 304 source : AC7 12) chain B residue 132 type sequence M description binding site for residue EDO B 304 source : AC7 13) chain B residue 139 type sequence C description binding site for residue EDO B 304 source : AC7 14) chain B residue 98 type BINDING sequence L description in other chain => ECO:0000269|PubMed:17052728 source Swiss-Prot : SWS_FT_FI3 15) chain B residue 133 type BINDING sequence D description in other chain => ECO:0000269|PubMed:17052728 source Swiss-Prot : SWS_FT_FI3 16) chain B residue 45 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:27257257 source Swiss-Prot : SWS_FT_FI7 17) chain B residue 74 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI8 18) chain B 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 B 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 B 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 B 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 22) chain B 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 23) chain B 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 24) chain B 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 25) chain B 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 26) chain B 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

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