eF-site ID 1rk2-A PDB Code 1rk2 Chain A click to enlarge Title E. COLI RIBOKINASE COMPLEXED WITH RIBOSE AND ADP, SOLVED IN SPACE GROUP P212121 Classification TRANSFERASE Compound RIBOKINASE Source null (RBSK_ECOLI) Sequence A:  AGSLVVLGSINADHILNLQSFPTPGETVTGNHYQVAFGGK GANQAVAAGRSGANIAFIACTGDDSIGESVRQQLATDNID ITPVSVIKGESTGVALIFVNGEGENVIGIHAGANAALSPA LVEAQRERIANASALLMQLESPLESVMAAAKIAHQNKTIV ALNPAPARELPDELLALVDIITPNETEAEKLTGIRVENDE DAAKAAQVLHEKGIRTVLITLGSRGVWASVNGEGQRVPGF RVQAVDTIAAGDTFNGALITALLEEKPLPEAIRFAHAAAA IAVTRKGAQPSVPWREEIDAFLDRQ Description Functional site 1) chain A 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 2) chain A 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 3) chain A 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 4) chain A 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 5) chain A 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 6) chain A 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 7) chain A 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 8) chain A 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 9) chain A residue 249 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021 source Swiss-Prot : SWS_FT_FI3 10) chain A residue 251 type BINDING sequence I description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021 source Swiss-Prot : SWS_FT_FI3 11) chain A residue 285 type BINDING sequence A description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021 source Swiss-Prot : SWS_FT_FI3 12) chain A residue 288 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021 source Swiss-Prot : SWS_FT_FI3 13) chain A residue 290 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021 source Swiss-Prot : SWS_FT_FI3 14) chain A residue 294 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021 source Swiss-Prot : SWS_FT_FI3 15) chain A 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 16) chain A residue 252 type catalytic sequence A description 663 source MCSA : MCSA1 17) chain A residue 253 type catalytic sequence A description 663 source MCSA : MCSA1 18) chain A residue 254 type catalytic sequence G description 663 source MCSA : MCSA1 19) chain A residue 255 type catalytic sequence D description 663 source MCSA : MCSA1 20) chain A residue 249-262 type prosite sequence DTIAAGDTFNGALI description PFKB_KINASES_2 pfkB family of carbohydrate kinases signature 2. DTiAAGDtfnGALI source prosite : PS00584

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