eF-site ID 1rk2-B PDB Code 1rk2 Chain B 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 B:  QNAGSLVVLGSINADHILNLQSFPTPGETVTGNHYQVAFG GKGANQAVAAGRSGANIAFIACTGDDSIGESVRQQLATDN IDITPVSVIKGESTGVALIFVNGEGENVIGIHAGANAALS PALVEAQRERIANASALLMQLESPLESVMAAAKIAHQNKT IVALNPAPARELPDELLALVDIITPNETEAEKLTGIRVEN DEDAAKAAQVLHEKGIRTVLITLGSRGVWASVNGEGQRVP GFRVQAVDTIAAGDTFNGALITALLEEKPLPEAIRFAHAA AAIAVTRKGAQPSVPWREEIDAFLDRQ Description Functional site 1) chain B residue 252 type catalytic sequence A description 663 source MCSA : MCSA2 2) chain B residue 253 type catalytic sequence A description 663 source MCSA : MCSA2 3) chain B residue 254 type catalytic sequence G description 663 source MCSA : MCSA2 4) chain B residue 255 type catalytic sequence D description 663 source MCSA : MCSA2 5) chain B 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 B 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 7) chain B 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 8) chain B 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 9) chain B 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 10) chain B 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 11) chain B 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 12) chain B 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 13) chain B residue 288 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021 source Swiss-Prot : SWS_FT_FI3 14) chain B residue 290 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021 source Swiss-Prot : SWS_FT_FI3 15) chain B residue 294 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021 source Swiss-Prot : SWS_FT_FI3 16) chain B residue 249 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021 source Swiss-Prot : SWS_FT_FI3 17) chain B residue 251 type BINDING sequence I description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021 source Swiss-Prot : SWS_FT_FI3 18) chain B residue 285 type BINDING sequence A description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021 source Swiss-Prot : SWS_FT_FI3 19) chain B 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

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