eF-site ID 4kx3-A PDB Code 4kx3 Chain A click to enlarge Title Structure of murine cytosolic 5'-nucleotidase III complexed with thymidine monophosphate Classification HYDROLASE Compound Cytosolic 5'-nucleotidase 3 Source Mus musculus (Mouse) (5NT3_MOUSE) Sequence A:  AVHLKMMPEFQKSSVRIKNPTRVEEIICGLIKGGAAKLQI ITDFNMTLSRFSYNGKRCPTCHNIIDNCKLVTDECRRKLL QLKEQYYAIEVDPVLTVEEKFPYMVEWYTKSHGLLIEQGI PKAKLKEIVADSDVMLKEGYENFFGKLQQHGIPVFIFSAG IGDVLEEVIRQAGVYHSNVKVVSNFMDFDENGVLKGFKGE LIHVFNKHDGALKNTDYFSQLKDNSNIILLGDSQGDLRMA DGVANVEHILKIGYLNDRVDELLEKYMDSYDIVLVKEESL EVVNSILQKTL Description Functional site 1) chain A residue 49 type sequence D description BINDING SITE FOR RESIDUE DT A 301 source : AC1 2) chain A residue 50 type sequence F description BINDING SITE FOR RESIDUE DT A 301 source : AC1 3) chain A residue 51 type sequence N description BINDING SITE FOR RESIDUE DT A 301 source : AC1 4) chain A residue 66 type sequence T description BINDING SITE FOR RESIDUE DT A 301 source : AC1 5) chain A residue 68 type sequence H description BINDING SITE FOR RESIDUE DT A 301 source : AC1 6) chain A residue 69 type sequence N description BINDING SITE FOR RESIDUE DT A 301 source : AC1 7) chain A residue 96 type sequence E description BINDING SITE FOR RESIDUE DT A 301 source : AC1 8) chain A residue 113 type sequence W description BINDING SITE FOR RESIDUE DT A 301 source : AC1 9) chain A residue 114 type sequence Y description BINDING SITE FOR RESIDUE DT A 301 source : AC1 10) chain A residue 117 type sequence S description BINDING SITE FOR RESIDUE DT A 301 source : AC1 11) chain A residue 164 type sequence S description BINDING SITE FOR RESIDUE DT A 301 source : AC1 12) chain A residue 165 type sequence A description BINDING SITE FOR RESIDUE DT A 301 source : AC1 13) chain A residue 166 type sequence G description BINDING SITE FOR RESIDUE DT A 301 source : AC1 14) chain A residue 213 type sequence K description BINDING SITE FOR RESIDUE DT A 301 source : AC1 15) chain A residue 49 type sequence D description BINDING SITE FOR RESIDUE MG A 302 source : AC2 16) chain A residue 51 type sequence N description BINDING SITE FOR RESIDUE MG A 302 source : AC2 17) chain A residue 238 type sequence D description BINDING SITE FOR RESIDUE MG A 302 source : AC2 18) chain A residue 24 type sequence K description BINDING SITE FOR RESIDUE EDO A 303 source : AC3 19) chain A residue 26 type sequence P description BINDING SITE FOR RESIDUE EDO A 303 source : AC3 20) chain A residue 27 type sequence T description BINDING SITE FOR RESIDUE EDO A 303 source : AC3 21) chain A residue 28 type sequence R description BINDING SITE FOR RESIDUE EDO A 303 source : AC3 22) chain A residue 31 type sequence E description BINDING SITE FOR RESIDUE EDO A 303 source : AC3 23) chain A residue 63 type sequence R description BINDING SITE FOR RESIDUE EDO A 304 source : AC4 24) chain A residue 69 type sequence N description BINDING SITE FOR RESIDUE EDO A 304 source : AC4 25) chain A residue 89 type sequence K description BINDING SITE FOR RESIDUE EDO A 304 source : AC4 26) chain A residue 154 type sequence Q description BINDING SITE FOR RESIDUE EDO A 305 source : AC5 27) chain A residue 157 type sequence G description BINDING SITE FOR RESIDUE EDO A 305 source : AC5 28) chain A residue 176 type sequence R description BINDING SITE FOR RESIDUE EDO A 305 source : AC5 29) chain A residue 183 type sequence S description BINDING SITE FOR RESIDUE EDO A 305 source : AC5 30) chain A residue 184 type sequence N description BINDING SITE FOR RESIDUE EDO A 305 source : AC5 31) chain A residue 34 type sequence C description BINDING SITE FOR RESIDUE BME A 306 source : AC6 32) chain A residue 38 type sequence K description BINDING SITE FOR RESIDUE BME A 306 source : AC6 33) chain A residue 59 type sequence Y description BINDING SITE FOR RESIDUE BME A 307 source : AC7 34) chain A residue 62 type sequence K description BINDING SITE FOR RESIDUE BME A 307 source : AC7 35) chain A residue 63 type sequence R description BINDING SITE FOR RESIDUE BME A 307 source : AC7 36) chain A residue 64 type sequence C description BINDING SITE FOR RESIDUE BME A 307 source : AC7 37) chain A residue 139 type sequence D description BINDING SITE FOR RESIDUE BME A 307 source : AC7 38) chain A residue 206 type sequence E description BINDING SITE FOR RESIDUE EPE A 308 source : AC8 39) chain A residue 294 type sequence Q description BINDING SITE FOR RESIDUE EPE A 308 source : AC8 40) chain A residue 295 type sequence K description BINDING SITE FOR RESIDUE EPE A 308 source : AC8 41) chain A residue 297 type sequence L description BINDING SITE FOR RESIDUE EPE A 308 source : AC8 42) chain A residue 41 type sequence A description BINDING SITE FOR RESIDUE EDO A 309 source : AC9 43) chain A residue 42 type sequence A description BINDING SITE FOR RESIDUE EDO A 309 source : AC9 44) chain A residue 156 type sequence H description BINDING SITE FOR RESIDUE EDO A 309 source : AC9 45) chain A residue 157 type sequence G description BINDING SITE FOR RESIDUE EDO A 309 source : AC9 46) chain A residue 230 type sequence N description BINDING SITE FOR RESIDUE EDO A 309 source : AC9 47) chain A residue 83 type ACT_SITE sequence R description Nucleophile => ECO:0000269|PubMed:16672222 source Swiss-Prot : SWS_FT_FI1 48) chain A residue 85 type ACT_SITE sequence L description Proton donor => ECO:0000269|PubMed:16672222 source Swiss-Prot : SWS_FT_FI2 49) chain A residue 83 type BINDING sequence R description BINDING => ECO:0000269|PubMed:16672222 source Swiss-Prot : SWS_FT_FI3 50) chain A residue 85 type BINDING sequence L description BINDING => ECO:0000269|PubMed:16672222 source Swiss-Prot : SWS_FT_FI3 51) chain A residue 198 type BINDING sequence G description BINDING => ECO:0000269|PubMed:16672222 source Swiss-Prot : SWS_FT_FI3 52) chain A residue 247 type BINDING sequence D description BINDING => ECO:0000269|PubMed:16672222 source Swiss-Prot : SWS_FT_FI3 53) chain A residue 272 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:16672222 source Swiss-Prot : SWS_FT_FI3 54) chain A residue 130 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:Q9W197 source Swiss-Prot : SWS_FT_FI4 55) chain A residue 151 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q9W197 source Swiss-Prot : SWS_FT_FI4 56) chain A residue 273 type MOD_RES sequence M description Phosphoserine => ECO:0007744|PubMed:21183079 source Swiss-Prot : SWS_FT_FI5

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