eF-site ID 6ilt-AB PDB Code 6ilt Chain A, B click to enlarge Title Structure of Arabidopsis thaliana Ribokinase complexed with ATP and Magnesium ion Classification TRANSFERASE Compound Ribokinase Source (A1A6H3_ARATH) Sequence A:  MAPPLVVVGSANADIYVEIERLPKEGETISAKTGQTLAGG KGANQAACGAKLMYPTYFVGRLGEDAHGKLIAEALGDDGC GVHLDYVRSVNNEPTGHAVVMLQSDGQNSIIIVGGANMKA WPEIMSDDDLEIVRNAGIVLLQREIPDSINIQVAKAVKKA GVPVILDVGGMDTPIPNELLDSIDILSPNETELSRLTGMP TETFEQISQAVAKCHKLGVKQVLVKLGSKGSALFIQGEKP IQQSIIPAAQVVDTTGAGDTFTAAFAVAMVEGKSHEECLR FAAAAASLCVQVKGAIPSMPDRKSVLKLLKFS B:  MAPPLVVVGSANADIYVEIERLPKEGETISAKTGQTLAGG KGANQAACGAKLMYPTYFVGRLGEDAHGKLIAEALGDDGC GVHLDYVRSVNNEPTGHAVVMLQSDGQNSIIIVGGANMKA WPEIMSDDDLEIVRNAGIVLLQREIPDSINIQVAKAVKKA GVPVILDVGGMDTPIPNELLDSIDILSPNETELSRLTGMP TETFEQISQAVAKCHKLGVKQVLVKLGSKGSALFIQGEKP IQQSIIPAAQVVDTTGAGDTFTAAFAVAMVEGKSHEECLR FAAAAASLCVQVKGAIPSMPDRKSVLKLLKFSI Description Functional site 1) chain A residue 255 type sequence N description binding site for residue ATP A 401 source : AC1 2) chain A residue 291 type sequence K description binding site for residue ATP A 401 source : AC1 3) chain A residue 292 type sequence L description binding site for residue ATP A 401 source : AC1 4) chain A residue 293 type sequence G description binding site for residue ATP A 401 source : AC1 5) chain A residue 296 type sequence G description binding site for residue ATP A 401 source : AC1 6) chain A residue 311 type sequence I description binding site for residue ATP A 401 source : AC1 7) chain A residue 323 type sequence A description binding site for residue ATP A 401 source : AC1 8) chain A residue 324 type sequence G description binding site for residue ATP A 401 source : AC1 9) chain A residue 352 type sequence A description binding site for residue ATP A 401 source : AC1 10) chain A residue 107 type sequence K description binding site for residue MG A 403 source : AC3 11) chain A residue 319 type sequence D description binding site for residue NA A 404 source : AC4 12) chain A residue 321 type sequence T description binding site for residue NA A 404 source : AC4 13) chain A residue 355 type sequence C description binding site for residue NA A 404 source : AC4 14) chain A residue 358 type sequence V description binding site for residue NA A 404 source : AC4 15) chain A residue 360 type sequence G description binding site for residue NA A 404 source : AC4 16) chain A residue 364 type sequence S description binding site for residue NA A 404 source : AC4 17) chain B residue 255 type sequence N description binding site for residue ATP B 401 source : AC5 18) chain B residue 291 type sequence K description binding site for residue ATP B 401 source : AC5 19) chain B residue 292 type sequence L description binding site for residue ATP B 401 source : AC5 20) chain B residue 293 type sequence G description binding site for residue ATP B 401 source : AC5 21) chain B residue 296 type sequence G description binding site for residue ATP B 401 source : AC5 22) chain B residue 312 type sequence I description binding site for residue ATP B 401 source : AC5 23) chain B residue 317 type sequence V description binding site for residue ATP B 401 source : AC5 24) chain B residue 324 type sequence G description binding site for residue ATP B 401 source : AC5 25) chain B residue 352 type sequence A description binding site for residue ATP B 401 source : AC5 26) chain B residue 107 type sequence K description binding site for residue MG B 403 source : AC7 27) chain B residue 319 type sequence D description binding site for residue NA B 404 source : AC8 28) chain B residue 321 type sequence T description binding site for residue NA B 404 source : AC8 29) chain B residue 355 type sequence C description binding site for residue NA B 404 source : AC8 30) chain B residue 358 type sequence V description binding site for residue NA B 404 source : AC8 31) chain B residue 360 type sequence G description binding site for residue NA B 404 source : AC8 32) chain B residue 364 type sequence S description binding site for residue NA B 404 source : AC8 33) chain A residue 325 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_03215 source Swiss-Prot : SWS_FT_FI1 34) chain B residue 325 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_03215 source Swiss-Prot : SWS_FT_FI1 35) chain A residue 78 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_03215 source Swiss-Prot : SWS_FT_FI2 36) chain A residue 355 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_03215 source Swiss-Prot : SWS_FT_FI2 37) chain A residue 358 type BINDING sequence V description BINDING => ECO:0000255|HAMAP-Rule:MF_03215 source Swiss-Prot : SWS_FT_FI2 38) chain A residue 360 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03215 source Swiss-Prot : SWS_FT_FI2 39) chain A residue 364 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_03215 source Swiss-Prot : SWS_FT_FI2 40) chain B residue 78 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_03215 source Swiss-Prot : SWS_FT_FI2 41) chain B residue 106 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03215 source Swiss-Prot : SWS_FT_FI2 42) chain B residue 210 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_03215 source Swiss-Prot : SWS_FT_FI2 43) chain B residue 255 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_03215 source Swiss-Prot : SWS_FT_FI2 44) chain B residue 291 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_03215 source Swiss-Prot : SWS_FT_FI2 45) chain B residue 319 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_03215 source Swiss-Prot : SWS_FT_FI2 46) chain A residue 106 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03215 source Swiss-Prot : SWS_FT_FI2 47) chain B residue 321 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_03215 source Swiss-Prot : SWS_FT_FI2 48) chain B residue 324 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03215 source Swiss-Prot : SWS_FT_FI2 49) chain B residue 325 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_03215 source Swiss-Prot : SWS_FT_FI2 50) chain B residue 355 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_03215 source Swiss-Prot : SWS_FT_FI2 51) chain B residue 358 type BINDING sequence V description BINDING => ECO:0000255|HAMAP-Rule:MF_03215 source Swiss-Prot : SWS_FT_FI2 52) chain B residue 360 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03215 source Swiss-Prot : SWS_FT_FI2 53) chain B residue 364 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_03215 source Swiss-Prot : SWS_FT_FI2 54) chain A residue 210 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_03215 source Swiss-Prot : SWS_FT_FI2 55) chain A residue 255 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_03215 source Swiss-Prot : SWS_FT_FI2 56) chain A residue 291 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_03215 source Swiss-Prot : SWS_FT_FI2 57) chain A residue 319 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_03215 source Swiss-Prot : SWS_FT_FI2 58) chain A residue 321 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_03215 source Swiss-Prot : SWS_FT_FI2 59) chain A residue 324 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03215 source Swiss-Prot : SWS_FT_FI2 60) chain A residue 325 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_03215 source Swiss-Prot : SWS_FT_FI2 61) chain A residue 319-332 type prosite sequence DTTGAGDTFTAAFA description PFKB_KINASES_2 pfkB family of carbohydrate kinases signature 2. DTtGAGDtftAAFA source prosite : PS00584

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