eF-site ID 5qjd-ABCD PDB Code 5qjd Chain A, B, C, 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 Z240297434 Classification HYDROLASE Compound ADP-sugar pyrophosphatase Source (NUDT5_HUMAN) Sequence A:  KQYIISEELISEGKWVKLEKTTYMDPTGKTRTWESVKRTT RKEQTADGVAVIPVLQRTLHYECIVLVKQFRPPMGGYCIE FPAGLIDDGETPEAAALRELEEETGYKGDIAECSPAVCMD PGLSNCTIHIVTVTINGDDAENARPKPKPGDGEFVEVISL PKNDLLQRLDALVAEEHLTVDARVYSYALALKHA B:  KQYIISEELISEGKWVKLEKTTYMDPTGKTRTWESVKRTT RKQTADGVAVIPVLQRTLHYECIVLVKQFRPPMGGYCIEF PAGLIDDGETPEAAALRELEEETGYKGDIAECSPAVCMDP GLSNCTIHIVTVTINGDDAENARPKPKPGDGEFVEVISLP KNDLLQRLDALVAEEHLTVDARVYSYALALKHAN C:  QYIISEELISEGKWVKLEKTTYMDPTGKTRTWESVKRTTR KQTADGVAVIPVLQRTLHYECIVLVKQFRPPMGGYCIEFP AGLIDDGETPEAAALRELEEETGYKGDIAECSPAVCMDPG LSNCTIHIVTVTINGDDAENARPKPKPGDGEFVEVISLPK NDLLQRLDALVAEEHLTVDARVYSYALALKHA D:  KQYIISEELISEGKWVKLEKTTYMDPTGKTRTWESVKRTT ADGVAVIPVLQRTLHYECIVLVKQFRPPMGGYCIEFPAGL IDDGETPEAAALRELEEETGYKGDIAECSPAVCMDPGLSN CTIHIVTVTINGDDAENARPKPKPGDGEFVEVISLPKNDL LQRLDALVAEEHLTVDARVYSYALALKHAN 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 46 type sequence W description binding site for residue K0M A 304 source : AC3 7) chain A residue 47 type sequence E description binding site for residue K0M A 304 source : AC3 8) chain B residue 28 type sequence W description binding site for residue K0M A 304 source : AC3 9) chain A residue 51 type sequence R description binding site for residue EDO A 305 source : AC4 10) chain A residue 139 type sequence C description binding site for residue EDO A 305 source : AC4 11) chain B residue 133 type sequence D description binding site for residue EDO A 305 source : AC4 12) chain B residue 69 type sequence Q description binding site for residue EDO B 301 source : AC5 13) chain B residue 149 type sequence N description binding site for residue EDO B 301 source : AC5 14) chain B residue 151 type sequence D description binding site for residue EDO B 301 source : AC5 15) chain B residue 96 type sequence A description binding site for residue MG B 302 source : AC6 16) chain B residue 116 type sequence E description binding site for residue MG B 302 source : AC6 17) chain B residue 112 type sequence E description binding site for residue MG B 303 source : AC7 18) chain B residue 115 type sequence E description binding site for residue MG B 303 source : AC7 19) chain B residue 166 type sequence E description binding site for residue MG B 303 source : AC7 20) chain C residue 122 type sequence D description binding site for residue EDO C 301 source : AC8 21) chain C residue 152 type sequence D description binding site for residue EDO C 301 source : AC8 22) chain C residue 154 type sequence E description binding site for residue EDO C 301 source : AC8 23) chain C residue 155 type sequence N description binding site for residue EDO C 301 source : AC8 24) chain C residue 96 type sequence A description binding site for residue MG C 302 source : AC9 25) chain C residue 97 type sequence G description binding site for residue MG C 302 source : AC9 26) chain C residue 112 type sequence E description binding site for residue MG C 302 source : AC9 27) chain C residue 116 type sequence E description binding site for residue MG C 302 source : AC9 28) chain C residue 166 type sequence E description binding site for residue MG C 302 source : AC9 29) chain C residue 96 type sequence A description binding site for residue MG C 303 source : AD1 30) chain C residue 116 type sequence E description binding site for residue MG C 303 source : AD1 31) chain C residue 45 type sequence T description binding site for residue K0M C 304 source : AD2 32) chain C residue 46 type sequence W description binding site for residue K0M C 304 source : AD2 33) chain C residue 47 type sequence E description binding site for residue K0M C 304 source : AD2 34) chain C residue 135 type sequence G description binding site for residue K0M C 304 source : AD2 35) chain D residue 28 type sequence W description binding site for residue K0M C 304 source : AD2 36) chain D residue 29 type sequence V description binding site for residue K0M C 304 source : AD2 37) chain D residue 164 type sequence D description binding site for residue K0M C 304 source : AD2 38) chain C residue 51 type sequence R description binding site for residue EDO C 305 source : AD3 39) chain C residue 132 type sequence M description binding site for residue EDO C 305 source : AD3 40) chain C residue 139 type sequence C description binding site for residue EDO C 305 source : AD3 41) chain D residue 133 type sequence D description binding site for residue EDO C 305 source : AD3 42) chain D residue 96 type sequence A description binding site for residue MG D 301 source : AD4 43) chain D residue 116 type sequence E description binding site for residue MG D 301 source : AD4 44) chain D residue 96 type sequence A description binding site for residue MG D 302 source : AD5 45) chain D residue 97 type sequence G description binding site for residue MG D 302 source : AD5 46) chain D residue 112 type sequence E description binding site for residue MG D 302 source : AD5 47) chain D residue 116 type sequence E description binding site for residue MG D 302 source : AD5 48) chain D residue 166 type sequence E description binding site for residue MG D 302 source : AD5 49) chain C residue 133 type sequence D description binding site for residue EDO D 303 source : AD6 50) chain D residue 51 type sequence R description binding site for residue EDO D 303 source : AD6 51) chain D residue 132 type sequence M description binding site for residue EDO D 303 source : AD6 52) chain D residue 139 type sequence C description binding site for residue EDO D 303 source : AD6 53) chain A residue 97-118 type prosite sequence GLIDDGETPEAAALRELEEETG description NUDIX_BOX Nudix box signature. GliddgEtpeaAAlRELeEEtG source prosite : PS00893 54) 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 55) 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 56) 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 57) 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 58) 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 59) 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 60) 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 61) 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 62) 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 63) 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 64) 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 65) 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 66) 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 67) 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 68) 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 69) 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 70) 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 71) 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 72) 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 73) 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 74) 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 75) 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 76) 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 77) 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 78) 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 79) 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 80) 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 81) 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 82) 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 83) 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 84) 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 85) 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 86) chain A residue 98 type BINDING sequence L description in other chain => ECO:0000269|PubMed:17052728 source Swiss-Prot : SWS_FT_FI3 87) chain A residue 133 type BINDING sequence D description in other chain => ECO:0000269|PubMed:17052728 source Swiss-Prot : SWS_FT_FI3 88) chain B residue 98 type BINDING sequence L description in other chain => ECO:0000269|PubMed:17052728 source Swiss-Prot : SWS_FT_FI3 89) chain B residue 133 type BINDING sequence D description in other chain => ECO:0000269|PubMed:17052728 source Swiss-Prot : SWS_FT_FI3 90) chain C residue 98 type BINDING sequence L description in other chain => ECO:0000269|PubMed:17052728 source Swiss-Prot : SWS_FT_FI3 91) chain C residue 133 type BINDING sequence D description in other chain => ECO:0000269|PubMed:17052728 source Swiss-Prot : SWS_FT_FI3 92) chain D residue 98 type BINDING sequence L description in other chain => ECO:0000269|PubMed:17052728 source Swiss-Prot : SWS_FT_FI3 93) chain D residue 133 type BINDING sequence D description in other chain => ECO:0000269|PubMed:17052728 source Swiss-Prot : SWS_FT_FI3 94) chain A residue 45 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:27257257 source Swiss-Prot : SWS_FT_FI7 95) chain B residue 45 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:27257257 source Swiss-Prot : SWS_FT_FI7 96) chain C residue 45 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:27257257 source Swiss-Prot : SWS_FT_FI7 97) chain D residue 45 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:27257257 source Swiss-Prot : SWS_FT_FI7 98) chain A residue 74 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI8 99) chain B residue 74 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI8 100) chain C residue 74 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI8 101) chain D residue 74 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI8 102) 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 103) 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 104) 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 105) 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

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