eF-site ID 1rk2-C PDB Code 1rk2 Chain C click to enlarge Title E. COLI RIBOKINASE COMPLEXED WITH RIBOSE AND ADP, SOLVED IN SPACE GROUP P212121 Classification TRANSFERASE Compound RIBOKINASE Source Escherichia coli (strain K12) (RBSK_ECOLI) Sequence C:  AGSLVVLGSINADHILNLQSFPTPGETVTGNHYQVAFGGK GANQAVAAGRSGANIAFIACTGDDSIGESVRQQLATDNID ITPVSVIKGESTGVALIFVNGEGENVIGIHAGANAALSPA LVEAQRERIANASALLMQLESPLESVMAAAKIAHQNKTIV ALNPAPARELPDELLALVDIITPNETEAEKLTGIRVENDE DAAKAAQVLHEKGIRTVLITLGSRGVWASVNGEGQRVPGF RVQAVDTIAAGDTFNGALITALLEEKPLPEAIRFAHAAAA IAVTRKGAQPSVPWREEIDAFLDRQR Description Functional site 1) chain C residue 252 type catalytic sequence A description 663 source MCSA : MCSA3 2) chain C residue 253 type catalytic sequence A description 663 source MCSA : MCSA3 3) chain C residue 254 type catalytic sequence G description 663 source MCSA : MCSA3 4) chain C residue 255 type catalytic sequence D description 663 source MCSA : MCSA3 5) chain C residue 255 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021 source Swiss-Prot : SWS_FT_FI1 6) chain C residue 14 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409 source Swiss-Prot : SWS_FT_FI2 7) chain C residue 42 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409 source Swiss-Prot : SWS_FT_FI2 8) chain C residue 143 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409 source Swiss-Prot : SWS_FT_FI2 9) chain C residue 187 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409 source Swiss-Prot : SWS_FT_FI2 10) chain C residue 223 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409 source Swiss-Prot : SWS_FT_FI2 11) chain C residue 255 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409 source Swiss-Prot : SWS_FT_FI2 12) chain C residue 279 type BINDING sequence H description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409 source Swiss-Prot : SWS_FT_FI2 13) chain C residue 254 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021 source Swiss-Prot : SWS_FT_FI4 14) chain C residue 249 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021 source Swiss-Prot : SWS_FT_FI3 15) chain C residue 251 type BINDING sequence I description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021 source Swiss-Prot : SWS_FT_FI3 16) chain C residue 285 type BINDING sequence A description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021 source Swiss-Prot : SWS_FT_FI3 17) chain C residue 288 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021 source Swiss-Prot : SWS_FT_FI3 18) chain C residue 290 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021 source Swiss-Prot : SWS_FT_FI3 19) chain C residue 294 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021 source Swiss-Prot : SWS_FT_FI3

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