eF-site ID 4tti-D PDB Code 4tti Chain D click to enlarge Title Crystal structure of double mutant E. Coli purine nucleoside phosphorylase with 4 FMC molecules Classification TRANSFERASE Compound Purine nucleoside phosphorylase DeoD-type Source (DEOD_ECOLI) Sequence D:  ATPHINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVN NVRGMLGFTGTYKGRKISVMGHGMGIPSCSIYTKELITDF GVKKIIRVGSCGAVLPHVKLRDVVIGMGACTDSKVNRIRF KDHDFAAIADFDMVRNAVDAAKALGIDARVGNLFSADLFY SPDGEMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTIC TVSAHIRTHEQTTAAEAQTTFNDMIKIALESVLLGDK Description Functional site 1) chain D residue 4 type sequence H description binding site for residue FMC A 300 source : AC1 2) chain D residue 43 type sequence R description binding site for residue FMC A 300 source : AC1 3) chain D residue 43 type sequence R description binding site for residue PO4 A 301 source : AC2 4) chain D residue 20 type sequence G description binding site for residue PO4 D 301 source : AC8 5) chain D residue 87 type sequence R description binding site for residue PO4 D 301 source : AC8 6) chain D residue 89 type sequence G description binding site for residue PO4 D 301 source : AC8 7) chain D residue 90 type sequence S description binding site for residue PO4 D 301 source : AC8 8) chain D residue 64 type sequence M description binding site for residue FMC D 302 source : AC9 9) chain D residue 87 type sequence R description binding site for residue FMC D 302 source : AC9 10) chain D residue 90 type sequence S description binding site for residue FMC D 302 source : AC9 11) chain D residue 91 type sequence C description binding site for residue FMC D 302 source : AC9 12) chain D residue 92 type sequence G description binding site for residue FMC D 302 source : AC9 13) chain D residue 159 type sequence F description binding site for residue FMC D 302 source : AC9 14) chain D residue 178 type sequence V description binding site for residue FMC D 302 source : AC9 15) chain D residue 179 type sequence E description binding site for residue FMC D 302 source : AC9 16) chain D residue 180 type sequence M description binding site for residue FMC D 302 source : AC9 17) chain D residue 181 type sequence E description binding site for residue FMC D 302 source : AC9 18) chain D residue 97 type sequence H description binding site for residue SO4 D 303 source : AD1 19) chain D residue 149 type sequence R description binding site for residue SO4 D 303 source : AD1 20) chain D residue 204 type ACT_SITE sequence A description Proton donor => ECO:0000255|HAMAP-Rule:MF_01627, ECO:0000269|PubMed:30337572 source Swiss-Prot : SWS_FT_FI1 21) chain D 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 22) chain D 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 23) chain D 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 24) chain D 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 25) chain D 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 26) chain D 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 27) chain D 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 28) chain D residue 217 type SITE sequence A 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 29) chain D residue 26 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:18723842 source Swiss-Prot : SWS_FT_FI7 30) chain D residue 20 type catalytic sequence G description 375 source MCSA : MCSA4 31) chain D residue 24 type catalytic sequence R description 375 source MCSA : MCSA4 32) chain D residue 43 type catalytic sequence R description 375 source MCSA : MCSA4 33) chain D residue 87 type catalytic sequence R description 375 source MCSA : MCSA4 34) chain D residue 90 type catalytic sequence S description 375 source MCSA : MCSA4 35) chain D residue 204 type catalytic sequence A description 375 source MCSA : MCSA4 36) chain D residue 217 type catalytic sequence A description 375 source MCSA : MCSA4

Display surface Download Links