eF-site ID 1rkd-A PDB Code 1rkd Chain A click to enlarge Title E. COLI RIBOKINASE COMPLEXED WITH RIBOSE AND ADP Classification CARBOHYDRATE KINASE Compound RIBOKINASE Source Escherichia coli (strain K12) (RBSK_ECOLI) Sequence A:  AGSLVVLGSINADHILNLQSFPTPGETVTGNHYQVAFGGK GANQAVAAGRSGANIAFIACTGDDSIGESVRQQLATDNID ITPVSVIKGESTGVALIFVNGEGENVIGIHAGANAALSPA LVEAQRERIANASALLMQLESPLESVMAAAKIAHQNKTIV ALNPAPARELPDELLALVDIITPNETEAEKLTGIRVENDE DAAKAAQVLHEKGIRTVLITLGSRGVWASVNGEGQRVPGF RVQAVDTIAAGDTFNGALITALLEEKPLPEAIRFAHAAAA IAVTRKGAQPSVPWREEIDAFLDRQR Description Functional site 1) chain A residue 14 type sequence N description RESIDUES MAKING DIRECT HYDROGEN BONDS WITH RIBOSE. source : RB1 2) chain A residue 16 type sequence D description RESIDUES MAKING DIRECT HYDROGEN BONDS WITH RIBOSE. source : RB1 3) chain A residue 42 type sequence G description RESIDUES MAKING DIRECT HYDROGEN BONDS WITH RIBOSE. source : RB1 4) chain A residue 43 type sequence K description RESIDUES MAKING DIRECT HYDROGEN BONDS WITH RIBOSE. source : RB1 5) chain A residue 46 type sequence N description RESIDUES MAKING DIRECT HYDROGEN BONDS WITH RIBOSE. source : RB1 6) chain A residue 143 type sequence E description RESIDUES MAKING DIRECT HYDROGEN BONDS WITH RIBOSE. source : RB1 7) chain A residue 255 type sequence D description RESIDUES MAKING DIRECT HYDROGEN BONDS WITH RIBOSE. source : RB1 8) chain A residue 252 type sequence A description RESIDUES MAKING WATER-MEDIATED HYDROGEN BONDS WITH RIBOSE. source : RB2 9) chain A residue 254 type sequence G description RESIDUES MAKING WATER-MEDIATED HYDROGEN BONDS WITH RIBOSE. source : RB2 10) chain A residue 255 type sequence D description RESIDUES MAKING WATER-MEDIATED HYDROGEN BONDS WITH RIBOSE. source : RB2 11) chain A residue 98 type sequence A description RESIDUES WITHIN VAN DER WAALS DISTANCE OF RIBOSE. source : RB3 12) chain A residue 100 type sequence I description RESIDUES WITHIN VAN DER WAALS DISTANCE OF RIBOSE. source : RB3 13) chain A residue 110 type sequence I description RESIDUES WITHIN VAN DER WAALS DISTANCE OF RIBOSE. source : RB3 14) chain A residue 112 type sequence I description RESIDUES WITHIN VAN DER WAALS DISTANCE OF RIBOSE. source : RB3 15) chain A residue 251 type sequence I description RESIDUES WITHIN VAN DER WAALS DISTANCE OF RIBOSE. source : RB3 16) chain A residue 187 type sequence N description RESIDUES MAKING DIRECT HYDROGEN BONDS WITH ADP. source : AB1 17) chain A residue 223 type sequence T description RESIDUES MAKING DIRECT HYDROGEN BONDS WITH ADP. source : AB1 18) chain A residue 225 type sequence G description RESIDUES MAKING DIRECT HYDROGEN BONDS WITH ADP. source : AB1 19) chain A residue 280 type sequence A description RESIDUES MAKING DIRECT HYDROGEN BONDS WITH ADP. source : AB1 20) chain A residue 166 type sequence N description RESIDUES MAKING WATER-MEDIATED HYDROGEN BONDS WITH ADP. source : AB2 21) chain A residue 187 type sequence N description RESIDUES MAKING WATER-MEDIATED HYDROGEN BONDS WITH ADP. source : AB2 22) chain A residue 190 type sequence E description RESIDUES MAKING WATER-MEDIATED HYDROGEN BONDS WITH ADP. source : AB2 23) chain A residue 223 type sequence T description RESIDUES MAKING WATER-MEDIATED HYDROGEN BONDS WITH ADP. source : AB2 24) chain A residue 243 type sequence F description RESIDUES MAKING WATER-MEDIATED HYDROGEN BONDS WITH ADP. source : AB2 25) chain A residue 245 type sequence V description RESIDUES MAKING WATER-MEDIATED HYDROGEN BONDS WITH ADP. source : AB2 26) chain A residue 280 type sequence A description RESIDUES MAKING WATER-MEDIATED HYDROGEN BONDS WITH ADP. source : AB2 27) chain A residue 225 type sequence G description RESIDUES WITHIN VAN DER WAALS DISTANCE OF ADP. source : AB3 28) chain A residue 245 type sequence V description RESIDUES WITHIN VAN DER WAALS DISTANCE OF ADP. source : AB3 29) chain A residue 253 type sequence A description RESIDUES WITHIN VAN DER WAALS DISTANCE OF ADP. source : AB3 30) chain A residue 282 type sequence A description RESIDUES WITHIN VAN DER WAALS DISTANCE OF ADP. source : AB3 31) chain A residue 286 type sequence V description RESIDUES WITHIN VAN DER WAALS DISTANCE OF ADP. source : AB3 32) chain A residue 252 type catalytic sequence A description 663 source MCSA : MCSA1 33) chain A residue 253 type catalytic sequence A description 663 source MCSA : MCSA1 34) chain A residue 254 type catalytic sequence G description 663 source MCSA : MCSA1 35) chain A residue 255 type catalytic sequence D description 663 source MCSA : MCSA1 36) 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 37) 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 38) 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 39) 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 40) 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 41) 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 42) 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 43) 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 44) 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 45) 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 46) 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 47) 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 48) 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 49) 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 50) 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 51) 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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