eF-site ID 4ts9-A PDB Code 4ts9 Chain A click to enlarge Title Crystal structure of wild type E. Coli purine nucleoside phosphorylase with 6 FMC molecules Classification TRANSFERASE Compound Purine nucleoside phosphorylase DeoD-type Source ORGANISM_SCIENTIFIC: Escherichia coli; Sequence A:  ATPHINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVN NVRGMLGFTGTYKGRKISVMGHGMGIPSCSIYTKELITDF GVKKIIRVASCGAVLPHVKLRDVVIGMGACTDSKVNRIRF KDHDFAAIADFDMVRNAVDAAKALGIDARVGNLFSADLFY SPDGEMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTIC TVSDHIRTHEQTTAAERQTTFNDMIKIALESVLLGDK Description Functional site 1) chain A residue 64 type sequence M description binding site for residue FMC A 300 source : AC1 2) chain A residue 87 type sequence R description binding site for residue FMC A 300 source : AC1 3) chain A residue 90 type sequence S description binding site for residue FMC A 300 source : AC1 4) chain A residue 91 type sequence C description binding site for residue FMC A 300 source : AC1 5) chain A residue 92 type sequence G description binding site for residue FMC A 300 source : AC1 6) chain A residue 159 type sequence F description binding site for residue FMC A 300 source : AC1 7) chain A residue 178 type sequence V description binding site for residue FMC A 300 source : AC1 8) chain A residue 179 type sequence E description binding site for residue FMC A 300 source : AC1 9) chain A residue 180 type sequence M description binding site for residue FMC A 300 source : AC1 10) chain A residue 181 type sequence E description binding site for residue FMC A 300 source : AC1 11) chain A residue 203 type sequence S description binding site for residue FMC A 300 source : AC1 12) chain A residue 204 type sequence D description binding site for residue FMC A 300 source : AC1 13) chain A residue 217 type sequence R description binding site for residue FMC A 300 source : AC1 14) chain A residue 19 type sequence P description binding site for residue PO4 A 301 source : AC2 15) chain A residue 20 type sequence G description binding site for residue PO4 A 301 source : AC2 16) chain A residue 24 type sequence R description binding site for residue PO4 A 301 source : AC2 17) chain A residue 87 type sequence R description binding site for residue PO4 A 301 source : AC2 18) chain A residue 89 type sequence A description binding site for residue PO4 A 301 source : AC2 19) chain A residue 90 type sequence S description binding site for residue PO4 A 301 source : AC2 20) chain A residue 43 type sequence R description binding site for residue PO4 C 301 source : AC5 21) chain A residue 4 type sequence H description binding site for residue FMC C 302 source : AC6 22) chain A residue 43 type sequence R description binding site for residue FMC C 302 source : AC6 23) chain A residue 20 type catalytic sequence G description 375 source MCSA : MCSA1 24) chain A residue 24 type catalytic sequence R description 375 source MCSA : MCSA1 25) chain A residue 43 type catalytic sequence R description 375 source MCSA : MCSA1 26) chain A residue 87 type catalytic sequence R description 375 source MCSA : MCSA1 27) chain A residue 90 type catalytic sequence S description 375 source MCSA : MCSA1 28) chain A residue 204 type catalytic sequence D description 375 source MCSA : MCSA1 29) chain A residue 217 type catalytic sequence R description 375 source MCSA : MCSA1 30) chain A residue 20 type BINDING sequence G description in other chain => ECO:0000269|PubMed:11786017, ECO:0000269|PubMed:21672603, ECO:0000269|PubMed:30337572, ECO:0007744|PDB:1K9S, ECO:0007744|PDB:3ONV, ECO:0007744|PDB:3OOE, ECO:0007744|PDB:3OOH, ECO:0007744|PDB:3OPV, ECO:0007744|PDB:4TS3, ECO:0007744|PDB:4TS9, ECO:0007744|PDB:4TTA, ECO:0007744|PDB:4TTI, ECO:0007744|PDB:4TTJ source Swiss-Prot : SWS_FT_FI3 31) chain A residue 24 type BINDING sequence R description in other chain => ECO:0000269|PubMed:11786017, ECO:0000269|PubMed:21672603, ECO:0000269|PubMed:30337572, ECO:0007744|PDB:1K9S, ECO:0007744|PDB:3ONV, ECO:0007744|PDB:3OOE, ECO:0007744|PDB:3OOH, ECO:0007744|PDB:3OPV, ECO:0007744|PDB:4TS3, ECO:0007744|PDB:4TS9, ECO:0007744|PDB:4TTA, ECO:0007744|PDB:4TTI, ECO:0007744|PDB:4TTJ source Swiss-Prot : SWS_FT_FI3 32) chain A residue 87 type BINDING sequence R description in other chain => ECO:0000269|PubMed:11786017, ECO:0000269|PubMed:21672603, ECO:0000269|PubMed:30337572, ECO:0007744|PDB:1K9S, ECO:0007744|PDB:3ONV, ECO:0007744|PDB:3OOE, ECO:0007744|PDB:3OOH, ECO:0007744|PDB:3OPV, ECO:0007744|PDB:4TS3, ECO:0007744|PDB:4TS9, ECO:0007744|PDB:4TTA, ECO:0007744|PDB:4TTI, ECO:0007744|PDB:4TTJ source Swiss-Prot : SWS_FT_FI3 33) chain A residue 179 type BINDING sequence E description in other chain => ECO:0000305|PubMed:30337572, ECO:0007744|PDB:4TS3, ECO:0007744|PDB:4TS9, ECO:0007744|PDB:4TTA, ECO:0007744|PDB:4TTI, ECO:0007744|PDB:4TTJ source Swiss-Prot : SWS_FT_FI5 34) chain A residue 203 type BINDING sequence S description in other chain => ECO:0000305|PubMed:30337572, ECO:0007744|PDB:4TS3, ECO:0007744|PDB:4TS9, ECO:0007744|PDB:4TTA, ECO:0007744|PDB:4TTI, ECO:0007744|PDB:4TTJ source Swiss-Prot : SWS_FT_FI5 35) chain A residue 217 type SITE sequence R description Important for catalytic activity => ECO:0000255|HAMAP-Rule:MF_01627, ECO:0000269|PubMed:21672603, ECO:0000269|PubMed:30337572 source Swiss-Prot : SWS_FT_FI6 36) chain A residue 61-76 type prosite sequence GHGMGIPSCSIYTKEL description PNP_UDP_1 Purine and other phosphorylases family 1 signature. GhGMGiPScSIytkEL source prosite : PS01232 37) chain A residue 204 type ACT_SITE sequence D description Proton donor => ECO:0000255|HAMAP-Rule:MF_01627, ECO:0000269|PubMed:30337572 source Swiss-Prot : SWS_FT_FI1 38) chain A residue 26 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:18723842 source Swiss-Prot : SWS_FT_FI7 39) chain A residue 4 type BINDING sequence H description BINDING => ECO:0000305|PubMed:30337572, ECO:0007744|PDB:4TS3, ECO:0007744|PDB:4TS9, ECO:0007744|PDB:4TTA, ECO:0007744|PDB:4TTI, ECO:0007744|PDB:4TTJ source Swiss-Prot : SWS_FT_FI2 40) chain A residue 43 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11786017, ECO:0000269|PubMed:21672603, ECO:0000269|PubMed:30337572, ECO:0007744|PDB:1K9S, ECO:0007744|PDB:3ONV, ECO:0007744|PDB:3OOE, ECO:0007744|PDB:3OOH, ECO:0007744|PDB:3OPV, ECO:0007744|PDB:4TS3, ECO:0007744|PDB:4TS9, ECO:0007744|PDB:4TTA, ECO:0007744|PDB:4TTI, ECO:0007744|PDB:4TTJ source Swiss-Prot : SWS_FT_FI4

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