eF-site ID 1pke-ABC PDB Code 1pke Chain A, B, C click to enlarge Title Crystal Structure of E. coli purine nucleoside phosphorylase complexed with 2-fluoro-2'-deoxyadenosine and sulfate/phosphate Classification TRANSFERASE Compound Purine nucleoside phosphorylase DeoD-type Source ORGANISM_SCIENTIFIC: Escherichia coli O157:H7; Sequence A:  ATPHINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVN NVRGMLGFTGTYKGRKISVMGHGMGIPSCSIYTKELITDF GVKKIIRVGSCGAVLPHVKLRDVVIGMGACTDSKVNRIRF KDHDFAAIADFDMVRNAVDAAKALGIDARVGNLFSADLFY SPDGEMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTIC TVSDHIRTHEQTTAAERQTTFNDMIKIALESVLLGDK B:  ATPHINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVN NVRGMLGFTGTYKGRKISVMGHGMGIPSCSIYTKELITDF GVKKIIRVGSCGAVLPHVKLRDVVIGMGACTDSKVNRIRF KDHDFAAIADFDMVRNAVDAAKALGIDARVGNLFSADLFY SPDGEMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTIC TVSDHIRTHEQTTAAERQTTFNDMIKIALESVLLGDK C:  ATPHINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVN NVRGMLGFTGTYKGRKISVMGHGMGIPSCSIYTKELITDF GVKKIIRVGSCGAVLPHVKLRDVVIGMGACTDSKVNRIRF KDHDFAAIADFDMVRNAVDAAKALGIDARVGNLFSADLFY SPDGEMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTIC TVSDHIRTHEQTQTTFNDMIKIALESVLLGDK Description Functional site 1) chain A residue 20 type sequence G description BINDING SITE FOR RESIDUE PO4 A 449 source : AC1 2) chain A residue 43 type sequence R description BINDING SITE FOR RESIDUE PO4 A 449 source : AC1 3) chain A residue 87 type sequence R description BINDING SITE FOR RESIDUE PO4 A 449 source : AC1 4) chain A residue 89 type sequence G description BINDING SITE FOR RESIDUE PO4 A 449 source : AC1 5) chain A residue 90 type sequence S description BINDING SITE FOR RESIDUE PO4 A 449 source : AC1 6) chain A residue 4 type sequence H description BINDING SITE FOR RESIDUE 2FD A 446 source : AC2 7) chain A residue 43 type sequence R description BINDING SITE FOR RESIDUE 2FD A 446 source : AC2 8) chain A residue 90 type sequence S description BINDING SITE FOR RESIDUE 2FD A 446 source : AC2 9) chain A residue 91 type sequence C description BINDING SITE FOR RESIDUE 2FD A 446 source : AC2 10) chain A residue 92 type sequence G description BINDING SITE FOR RESIDUE 2FD A 446 source : AC2 11) chain A residue 159 type sequence F description BINDING SITE FOR RESIDUE 2FD A 446 source : AC2 12) chain A residue 178 type sequence V description BINDING SITE FOR RESIDUE 2FD A 446 source : AC2 13) chain A residue 179 type sequence E description BINDING SITE FOR RESIDUE 2FD A 446 source : AC2 14) chain A residue 180 type sequence M description BINDING SITE FOR RESIDUE 2FD A 446 source : AC2 15) chain A residue 181 type sequence E description BINDING SITE FOR RESIDUE 2FD A 446 source : AC2 16) chain A residue 204 type sequence D description BINDING SITE FOR RESIDUE 2FD A 446 source : AC2 17) chain B residue 20 type sequence G description BINDING SITE FOR RESIDUE PO4 B 450 source : AC3 18) chain B residue 87 type sequence R description BINDING SITE FOR RESIDUE PO4 B 450 source : AC3 19) chain B residue 89 type sequence G description BINDING SITE FOR RESIDUE PO4 B 450 source : AC3 20) chain B residue 90 type sequence S description BINDING SITE FOR RESIDUE PO4 B 450 source : AC3 21) chain C residue 43 type sequence R description BINDING SITE FOR RESIDUE PO4 B 450 source : AC3 22) chain B residue 64 type sequence M description BINDING SITE FOR RESIDUE 2FD B 447 source : AC4 23) chain B residue 90 type sequence S description BINDING SITE FOR RESIDUE 2FD B 447 source : AC4 24) chain B residue 91 type sequence C description BINDING SITE FOR RESIDUE 2FD B 447 source : AC4 25) chain B residue 92 type sequence G description BINDING SITE FOR RESIDUE 2FD B 447 source : AC4 26) chain B residue 159 type sequence F description BINDING SITE FOR RESIDUE 2FD B 447 source : AC4 27) chain B residue 178 type sequence V description BINDING SITE FOR RESIDUE 2FD B 447 source : AC4 28) chain B residue 180 type sequence M description BINDING SITE FOR RESIDUE 2FD B 447 source : AC4 29) chain B residue 181 type sequence E description BINDING SITE FOR RESIDUE 2FD B 447 source : AC4 30) chain B residue 204 type sequence D description BINDING SITE FOR RESIDUE 2FD B 447 source : AC4 31) chain C residue 4 type sequence H description BINDING SITE FOR RESIDUE 2FD B 447 source : AC4 32) chain C residue 43 type sequence R description BINDING SITE FOR RESIDUE 2FD B 447 source : AC4 33) chain B residue 43 type sequence R description BINDING SITE FOR RESIDUE PO4 C 451 source : AC5 34) chain C residue 20 type sequence G description BINDING SITE FOR RESIDUE PO4 C 451 source : AC5 35) chain C residue 24 type sequence R description BINDING SITE FOR RESIDUE PO4 C 451 source : AC5 36) chain C residue 87 type sequence R description BINDING SITE FOR RESIDUE PO4 C 451 source : AC5 37) chain C residue 89 type sequence G description BINDING SITE FOR RESIDUE PO4 C 451 source : AC5 38) chain C residue 90 type sequence S description BINDING SITE FOR RESIDUE PO4 C 451 source : AC5 39) chain B residue 4 type sequence H description BINDING SITE FOR RESIDUE 2FD C 448 source : AC6 40) chain B residue 43 type sequence R description BINDING SITE FOR RESIDUE 2FD C 448 source : AC6 41) chain C residue 90 type sequence S description BINDING SITE FOR RESIDUE 2FD C 448 source : AC6 42) chain C residue 91 type sequence C description BINDING SITE FOR RESIDUE 2FD C 448 source : AC6 43) chain C residue 92 type sequence G description BINDING SITE FOR RESIDUE 2FD C 448 source : AC6 44) chain C residue 159 type sequence F description BINDING SITE FOR RESIDUE 2FD C 448 source : AC6 45) chain C residue 178 type sequence V description BINDING SITE FOR RESIDUE 2FD C 448 source : AC6 46) chain C residue 179 type sequence E description BINDING SITE FOR RESIDUE 2FD C 448 source : AC6 47) chain C residue 180 type sequence M description BINDING SITE FOR RESIDUE 2FD C 448 source : AC6 48) chain C residue 181 type sequence E description BINDING SITE FOR RESIDUE 2FD C 448 source : AC6 49) chain C residue 204 type sequence D description BINDING SITE FOR RESIDUE 2FD C 448 source : AC6 50) chain A residue 204 type ACT_SITE sequence D description Proton donor => ECO:0000255|HAMAP-Rule:MF_01627 source Swiss-Prot : SWS_FT_FI1 51) chain B residue 204 type ACT_SITE sequence D description Proton donor => ECO:0000255|HAMAP-Rule:MF_01627 source Swiss-Prot : SWS_FT_FI1 52) chain C residue 204 type ACT_SITE sequence D description Proton donor => ECO:0000255|HAMAP-Rule:MF_01627 source Swiss-Prot : SWS_FT_FI1 53) chain A residue 4 type BINDING sequence H description BINDING => ECO:0000269|PubMed:12937174 source Swiss-Prot : SWS_FT_FI2 54) chain A residue 43 type BINDING sequence R description BINDING => ECO:0000269|PubMed:12937174 source Swiss-Prot : SWS_FT_FI2 55) chain B residue 4 type BINDING sequence H description BINDING => ECO:0000269|PubMed:12937174 source Swiss-Prot : SWS_FT_FI2 56) chain B residue 43 type BINDING sequence R description BINDING => ECO:0000269|PubMed:12937174 source Swiss-Prot : SWS_FT_FI2 57) chain C residue 4 type BINDING sequence H description BINDING => ECO:0000269|PubMed:12937174 source Swiss-Prot : SWS_FT_FI2 58) chain C residue 43 type BINDING sequence R description BINDING => ECO:0000269|PubMed:12937174 source Swiss-Prot : SWS_FT_FI2 59) chain A residue 20 type BINDING sequence G description in other chain => ECO:0000269|PubMed:12937174 source Swiss-Prot : SWS_FT_FI3 60) chain A residue 24 type BINDING sequence R description in other chain => ECO:0000269|PubMed:12937174 source Swiss-Prot : SWS_FT_FI3 61) chain A residue 87 type BINDING sequence R description in other chain => ECO:0000269|PubMed:12937174 source Swiss-Prot : SWS_FT_FI3 62) chain B residue 203 type BINDING sequence S description in other chain => ECO:0000269|PubMed:12937174 source Swiss-Prot : SWS_FT_FI3 63) chain C residue 20 type BINDING sequence G description in other chain => ECO:0000269|PubMed:12937174 source Swiss-Prot : SWS_FT_FI3 64) chain C residue 24 type BINDING sequence R description in other chain => ECO:0000269|PubMed:12937174 source Swiss-Prot : SWS_FT_FI3 65) chain C residue 87 type BINDING sequence R description in other chain => ECO:0000269|PubMed:12937174 source Swiss-Prot : SWS_FT_FI3 66) chain C residue 179 type BINDING sequence E description in other chain => ECO:0000269|PubMed:12937174 source Swiss-Prot : SWS_FT_FI3 67) chain C residue 203 type BINDING sequence S description in other chain => ECO:0000269|PubMed:12937174 source Swiss-Prot : SWS_FT_FI3 68) chain A residue 179 type BINDING sequence E description in other chain => ECO:0000269|PubMed:12937174 source Swiss-Prot : SWS_FT_FI3 69) chain A residue 203 type BINDING sequence S description in other chain => ECO:0000269|PubMed:12937174 source Swiss-Prot : SWS_FT_FI3 70) chain B residue 20 type BINDING sequence G description in other chain => ECO:0000269|PubMed:12937174 source Swiss-Prot : SWS_FT_FI3 71) chain B residue 24 type BINDING sequence R description in other chain => ECO:0000269|PubMed:12937174 source Swiss-Prot : SWS_FT_FI3 72) chain B residue 87 type BINDING sequence R description in other chain => ECO:0000269|PubMed:12937174 source Swiss-Prot : SWS_FT_FI3 73) chain B residue 179 type BINDING sequence E description in other chain => ECO:0000269|PubMed:12937174 source Swiss-Prot : SWS_FT_FI3 74) chain A residue 217 type SITE sequence R description Important for catalytic activity => ECO:0000255|HAMAP-Rule:MF_01627 source Swiss-Prot : SWS_FT_FI4 75) chain B residue 217 type SITE sequence R description Important for catalytic activity => ECO:0000255|HAMAP-Rule:MF_01627 source Swiss-Prot : SWS_FT_FI4 76) chain A residue 26 type MOD_RES sequence K description N6-acetyllysine => ECO:0000255|HAMAP-Rule:MF_01627 source Swiss-Prot : SWS_FT_FI5 77) chain B residue 26 type MOD_RES sequence K description N6-acetyllysine => ECO:0000255|HAMAP-Rule:MF_01627 source Swiss-Prot : SWS_FT_FI5 78) chain C residue 26 type MOD_RES sequence K description N6-acetyllysine => ECO:0000255|HAMAP-Rule:MF_01627 source Swiss-Prot : SWS_FT_FI5 79) chain A residue 61-76 type prosite sequence GHGMGIPSCSIYTKEL description PNP_UDP_1 Purine and other phosphorylases family 1 signature. GhGMGiPScSIytkEL source prosite : PS01232

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