eF-site ID 4ts9-C PDB Code 4ts9 Chain C 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 C:  ATPHINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVN NVRGMLGFTGTYKGRKISVMGHGMGIPSCSIYTKELITDF GVKKIIRVASCGAVLPHVKLRDVVIGMGACTDSKVNRIRF KDHDFAAIADFDMVRNAVDAAKALGIDARVGNLFSADLFY SPDGEMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTIC TVSDHIRTHEQTTAAERQTTFNDMIKIALESVLLGDK Description Functional site 1) chain C residue 4 type sequence H description binding site for residue FMC A 300 source : AC1 2) chain C residue 43 type sequence R description binding site for residue FMC A 300 source : AC1 3) chain C residue 43 type sequence R description binding site for residue PO4 A 301 source : AC2 4) chain C residue 20 type sequence G description binding site for residue PO4 C 301 source : AC5 5) chain C residue 87 type sequence R description binding site for residue PO4 C 301 source : AC5 6) chain C residue 89 type sequence A description binding site for residue PO4 C 301 source : AC5 7) chain C residue 90 type sequence S description binding site for residue PO4 C 301 source : AC5 8) chain C residue 87 type sequence R description binding site for residue FMC C 302 source : AC6 9) chain C residue 90 type sequence S description binding site for residue FMC C 302 source : AC6 10) chain C residue 91 type sequence C description binding site for residue FMC C 302 source : AC6 11) chain C residue 92 type sequence G description binding site for residue FMC C 302 source : AC6 12) chain C residue 159 type sequence F description binding site for residue FMC C 302 source : AC6 13) chain C residue 178 type sequence V description binding site for residue FMC C 302 source : AC6 14) chain C residue 179 type sequence E description binding site for residue FMC C 302 source : AC6 15) chain C residue 180 type sequence M description binding site for residue FMC C 302 source : AC6 16) chain C residue 181 type sequence E description binding site for residue FMC C 302 source : AC6 17) chain C residue 204 type sequence D description binding site for residue FMC C 302 source : AC6 18) chain C residue 20 type catalytic sequence G description 375 source MCSA : MCSA3 19) chain C residue 24 type catalytic sequence R description 375 source MCSA : MCSA3 20) chain C residue 43 type catalytic sequence R description 375 source MCSA : MCSA3 21) chain C residue 87 type catalytic sequence R description 375 source MCSA : MCSA3 22) chain C residue 90 type catalytic sequence S description 375 source MCSA : MCSA3 23) chain C residue 204 type catalytic sequence D description 375 source MCSA : MCSA3 24) chain C residue 217 type catalytic sequence R description 375 source MCSA : MCSA3 25) chain C 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 26) chain C 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 27) chain C 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 28) chain C 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 29) chain C 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 30) chain C 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 31) chain C 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 32) chain C 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 33) chain C 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 34) chain C residue 26 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:18723842 source Swiss-Prot : SWS_FT_FI7

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