eF-site ID 5qje-ABCD PDB Code 5qje 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 Z275181224 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 96 type sequence A description binding site for residue MG A 302 source : AC2 4) chain A residue 112 type sequence E description binding site for residue MG A 302 source : AC2 5) chain A residue 116 type sequence E description binding site for residue MG A 302 source : AC2 6) chain A residue 166 type sequence E description binding site for residue MG A 302 source : AC2 7) chain A residue 51 type sequence R description binding site for residue EDO A 304 source : AC3 8) chain A residue 139 type sequence C description binding site for residue EDO A 304 source : AC3 9) chain B residue 133 type sequence D description binding site for residue EDO A 304 source : AC3 10) chain B residue 69 type sequence Q description binding site for residue EDO B 301 source : AC4 11) chain B residue 149 type sequence N description binding site for residue EDO B 301 source : AC4 12) chain B residue 151 type sequence D description binding site for residue EDO B 301 source : AC4 13) chain B residue 96 type sequence A description binding site for residue MG B 302 source : AC5 14) chain B residue 116 type sequence E description binding site for residue MG B 302 source : AC5 15) chain B residue 112 type sequence E description binding site for residue MG B 303 source : AC6 16) chain B residue 116 type sequence E description binding site for residue MG B 303 source : AC6 17) chain B residue 166 type sequence E description binding site for residue MG B 303 source : AC6 18) chain A residue 28 type sequence W description binding site for residue K0P B 304 source : AC7 19) chain A residue 164 type sequence D description binding site for residue K0P B 304 source : AC7 20) chain A residue 165 type sequence G description binding site for residue K0P B 304 source : AC7 21) chain B residue 36 type sequence Y description binding site for residue K0P B 304 source : AC7 22) chain B residue 46 type sequence W description binding site for residue K0P B 304 source : AC7 23) chain B residue 47 type sequence E description binding site for residue K0P B 304 source : AC7 24) chain A residue 133 type sequence D description binding site for residue EDO B 305 source : AC8 25) chain B residue 51 type sequence R description binding site for residue EDO B 305 source : AC8 26) chain B residue 132 type sequence M description binding site for residue EDO B 305 source : AC8 27) chain B residue 139 type sequence C description binding site for residue EDO B 305 source : AC8 28) chain C residue 122 type sequence D description binding site for residue EDO C 301 source : AC9 29) chain C residue 152 type sequence D description binding site for residue EDO C 301 source : AC9 30) chain C residue 154 type sequence E description binding site for residue EDO C 301 source : AC9 31) chain C residue 155 type sequence N description binding site for residue EDO C 301 source : AC9 32) chain C residue 96 type sequence A description binding site for residue MG C 302 source : AD1 33) chain C residue 97 type sequence G description binding site for residue MG C 302 source : AD1 34) chain C residue 112 type sequence E description binding site for residue MG C 302 source : AD1 35) chain C residue 116 type sequence E description binding site for residue MG C 302 source : AD1 36) chain C residue 166 type sequence E description binding site for residue MG C 302 source : AD1 37) chain C residue 96 type sequence A description binding site for residue MG C 303 source : AD2 38) chain C residue 116 type sequence E description binding site for residue MG C 303 source : AD2 39) chain C residue 166 type sequence E description binding site for residue MG C 303 source : AD2 40) chain C residue 51 type sequence R description binding site for residue EDO C 304 source : AD3 41) chain C residue 132 type sequence M description binding site for residue EDO C 304 source : AD3 42) chain C residue 139 type sequence C description binding site for residue EDO C 304 source : AD3 43) chain D residue 133 type sequence D description binding site for residue EDO C 304 source : AD3 44) chain D residue 96 type sequence A description binding site for residue MG D 301 source : AD4 45) chain D residue 116 type sequence E description binding site for residue MG D 301 source : AD4 46) chain D residue 96 type sequence A description binding site for residue MG D 302 source : AD5 47) chain D residue 97 type sequence G description binding site for residue MG D 302 source : AD5 48) chain D residue 112 type sequence E description binding site for residue MG D 302 source : AD5 49) chain D residue 116 type sequence E description binding site for residue MG D 302 source : AD5 50) chain D residue 166 type sequence E description binding site for residue MG D 302 source : AD5 51) chain C residue 46 type sequence W description binding site for residue K0P D 303 source : AD6 52) chain C residue 47 type sequence E description binding site for residue K0P D 303 source : AD6 53) chain D residue 28 type sequence W description binding site for residue K0P D 303 source : AD6 54) chain D residue 51 type sequence R description binding site for residue K0P D 303 source : AD6 55) chain D residue 164 type sequence D description binding site for residue K0P D 303 source : AD6 56) chain D residue 165 type sequence G description binding site for residue K0P D 303 source : AD6 57) chain C residue 133 type sequence D description binding site for residue EDO D 304 source : AD7 58) chain D residue 51 type sequence R description binding site for residue EDO D 304 source : AD7 59) chain D residue 132 type sequence M description binding site for residue EDO D 304 source : AD7 60) chain D residue 139 type sequence C description binding site for residue EDO D 304 source : AD7 61) chain A residue 45 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:27257257 source Swiss-Prot : SWS_FT_FI7 62) chain B residue 45 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:27257257 source Swiss-Prot : SWS_FT_FI7 63) chain C residue 45 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:27257257 source Swiss-Prot : SWS_FT_FI7 64) chain D residue 45 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:27257257 source Swiss-Prot : SWS_FT_FI7 65) chain A residue 74 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI8 66) chain B residue 74 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI8 67) chain C residue 74 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI8 68) chain D residue 74 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI8 69) 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 70) 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 71) 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 72) 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 73) 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 74) 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 75) 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 76) 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 77) 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 78) 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 79) 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 80) 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 81) 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 82) 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 83) 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 84) 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 85) 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 86) 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 87) 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 88) 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 89) 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 90) 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 91) 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 92) 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 93) 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 94) 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 95) 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 96) 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 97) 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 98) 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 99) 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 100) 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 101) 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 102) 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 103) 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 104) 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 105) chain A residue 98 type BINDING sequence L description in other chain => ECO:0000269|PubMed:17052728 source Swiss-Prot : SWS_FT_FI3 106) chain A residue 133 type BINDING sequence D description in other chain => ECO:0000269|PubMed:17052728 source Swiss-Prot : SWS_FT_FI3 107) chain B residue 98 type BINDING sequence L description in other chain => ECO:0000269|PubMed:17052728 source Swiss-Prot : SWS_FT_FI3 108) chain B residue 133 type BINDING sequence D description in other chain => ECO:0000269|PubMed:17052728 source Swiss-Prot : SWS_FT_FI3 109) chain C residue 98 type BINDING sequence L description in other chain => ECO:0000269|PubMed:17052728 source Swiss-Prot : SWS_FT_FI3 110) chain C residue 133 type BINDING sequence D description in other chain => ECO:0000269|PubMed:17052728 source Swiss-Prot : SWS_FT_FI3 111) chain D residue 98 type BINDING sequence L description in other chain => ECO:0000269|PubMed:17052728 source Swiss-Prot : SWS_FT_FI3 112) chain D residue 133 type BINDING sequence D description in other chain => ECO:0000269|PubMed:17052728 source Swiss-Prot : SWS_FT_FI3 113) chain A residue 97-118 type prosite sequence GLIDDGETPEAAALRELEEETG description NUDIX_BOX Nudix box signature. GliddgEtpeaAAlRELeEEtG source prosite : PS00893

Display surface Download Links