eF-site ID 4ts9-B PDB Code 4ts9 Chain B 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 B:  ATPHINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVN NVRGMLGFTGTYKGRKISVMGHGMGIPSCSIYTKELITDF GVKKIIRVASCGAVLPHVKLRDVVIGMGACTDSKVNRIRF KDHDFAAIADFDMVRNAVDAAKALGIDARVGNLFSADLFY SPDGEMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTIC TVSDHIRTHEQTTAAERQTTFNDMIKIALESVLLGDK Description Functional site 1) chain B residue 20 type sequence G description binding site for residue PO4 B 301 source : AC3 2) chain B residue 43 type sequence R description binding site for residue PO4 B 301 source : AC3 3) chain B residue 87 type sequence R description binding site for residue PO4 B 301 source : AC3 4) chain B residue 89 type sequence A description binding site for residue PO4 B 301 source : AC3 5) chain B residue 90 type sequence S description binding site for residue PO4 B 301 source : AC3 6) chain B residue 4 type sequence H description binding site for residue FMC B 302 source : AC4 7) chain B residue 43 type sequence R description binding site for residue FMC B 302 source : AC4 8) chain B residue 64 type sequence M description binding site for residue FMC B 302 source : AC4 9) chain B residue 87 type sequence R description binding site for residue FMC B 302 source : AC4 10) chain B residue 90 type sequence S description binding site for residue FMC B 302 source : AC4 11) chain B residue 91 type sequence C description binding site for residue FMC B 302 source : AC4 12) chain B residue 92 type sequence G description binding site for residue FMC B 302 source : AC4 13) chain B residue 159 type sequence F description binding site for residue FMC B 302 source : AC4 14) chain B residue 178 type sequence V description binding site for residue FMC B 302 source : AC4 15) chain B residue 179 type sequence E description binding site for residue FMC B 302 source : AC4 16) chain B residue 180 type sequence M description binding site for residue FMC B 302 source : AC4 17) chain B residue 181 type sequence E description binding site for residue FMC B 302 source : AC4 18) chain B residue 204 type sequence D description binding site for residue FMC B 302 source : AC4 19) chain B residue 206 type sequence I description binding site for residue FMC B 302 source : AC4 20) chain B residue 20 type catalytic sequence G description 375 source MCSA : MCSA2 21) chain B residue 24 type catalytic sequence R description 375 source MCSA : MCSA2 22) chain B residue 43 type catalytic sequence R description 375 source MCSA : MCSA2 23) chain B residue 87 type catalytic sequence R description 375 source MCSA : MCSA2 24) chain B residue 90 type catalytic sequence S description 375 source MCSA : MCSA2 25) chain B residue 204 type catalytic sequence D description 375 source MCSA : MCSA2 26) chain B residue 217 type catalytic sequence R description 375 source MCSA : MCSA2 27) chain B 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 28) chain B 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 29) chain B 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 30) chain B 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 31) chain B 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 32) chain B 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 33) chain B 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 34) chain B 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 35) chain B 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 B residue 26 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:18723842 source Swiss-Prot : SWS_FT_FI7

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