eF-site ID 1mum-AB PDB Code 1mum Chain A, B click to enlarge Title Structure of the 2-Methylisocitrate Lyase (PrpB) from Escherichia coli Classification LYASE Compound 2-methylisocitrate lyase Source Escherichia coli (strain K12) (PRPB_ECOLI) Sequence A:  LHSPGKAFRAALTKENPLQIVGTINANHALLAQRAGYQAI YLSGGGVAAGSLGLPDLGISTLDDVLTDIRRITDVCSLPL LVDADIGFGSSAFNVARTVKSMIKAGAAGLHIEDQVGAKR CGHRPNKAIVSKEEMVDRIRAAVDAKTDPDFVIMARTDAL AVEGLDAAIERAQAYVEAGAEMLFPEAITELAMYRQFADA VQVPILANITEFGATPLFTTDELRSAHVAMALYPLSAFRA MNRAAEHVYNVLRQEGTQKSVIDTMQTRNELYESINYYQY EEKLDNLFA B:  LHSPGKAFRAALTKENPLQIVGTINANHALLAQRAGYQAI YLSGGGVAAGSLGLPDLGISTLDDVLTDIRRITDVCSLPL LVDADIGFGSSAFNVARTVKSMIKAGAAGLHIEDQVGAKR CGHRPNKAIVSKEEMVDRIRAAVDAKTDPDFVIMARTDAL AVEGLDAAIERAQAYVEAGAEMLFPEAITELAMYRQFADA VQVPILANITEFGATPLFTTDELRSAHVAMALYPLSAFRA MNRAAEHVYNVLRQEGTQKSVIDTMQTRNELYESINYYQY EEKLDNLFA Description Functional site 1) chain A residue 58 type sequence D description BINDING SITE FOR RESIDUE MG A 1001 source : AC1 2) chain A residue 87 type sequence D description BINDING SITE FOR RESIDUE MG A 1001 source : AC1 3) chain B residue 58 type sequence D description BINDING SITE FOR RESIDUE MG B 1002 source : AC2 4) chain B residue 87 type sequence D description BINDING SITE FOR RESIDUE MG B 1002 source : AC2 5) chain A residue 44 type catalytic sequence L description 182 source MCSA : MCSA1 6) chain A residue 211 type catalytic sequence I description 182 source MCSA : MCSA1 7) chain A residue 59 type catalytic sequence L description 182 source MCSA : MCSA1 8) chain A residue 86 type catalytic sequence A description 182 source MCSA : MCSA1 9) chain A residue 88 type catalytic sequence I description 182 source MCSA : MCSA1 10) chain A residue 114 type catalytic sequence I description 182 source MCSA : MCSA1 11) chain A residue 116 type catalytic sequence D description 182 source MCSA : MCSA1 12) chain A residue 124 type catalytic sequence G description 182 source MCSA : MCSA1 13) chain A residue 159 type catalytic sequence T description 182 source MCSA : MCSA1 14) chain A residue 189 type catalytic sequence A description 182 source MCSA : MCSA1 15) chain B residue 44 type catalytic sequence L description 182 source MCSA : MCSA2 16) chain B residue 211 type catalytic sequence I description 182 source MCSA : MCSA2 17) chain B residue 59 type catalytic sequence L description 182 source MCSA : MCSA2 18) chain B residue 86 type catalytic sequence A description 182 source MCSA : MCSA2 19) chain B residue 88 type catalytic sequence I description 182 source MCSA : MCSA2 20) chain B residue 114 type catalytic sequence I description 182 source MCSA : MCSA2 21) chain B residue 116 type catalytic sequence D description 182 source MCSA : MCSA2 22) chain B residue 124 type catalytic sequence G description 182 source MCSA : MCSA2 23) chain B residue 159 type catalytic sequence T description 182 source MCSA : MCSA2 24) chain B residue 189 type catalytic sequence A description 182 source MCSA : MCSA2 25) chain A residue 46 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_01939, ECO:0000269|PubMed:15723538 source Swiss-Prot : SWS_FT_FI1 26) chain B residue 159 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_01939, ECO:0000269|PubMed:15723538 source Swiss-Prot : SWS_FT_FI1 27) chain B residue 189 type BINDING sequence A description BINDING => ECO:0000255|HAMAP-Rule:MF_01939, ECO:0000269|PubMed:15723538 source Swiss-Prot : SWS_FT_FI1 28) chain B residue 211 type BINDING sequence I description BINDING => ECO:0000255|HAMAP-Rule:MF_01939, ECO:0000269|PubMed:15723538 source Swiss-Prot : SWS_FT_FI1 29) chain B residue 242 type BINDING sequence A description BINDING => ECO:0000255|HAMAP-Rule:MF_01939, ECO:0000269|PubMed:15723538 source Swiss-Prot : SWS_FT_FI1 30) chain B residue 271 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_01939, ECO:0000269|PubMed:15723538 source Swiss-Prot : SWS_FT_FI1 31) chain A residue 124 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_01939, ECO:0000269|PubMed:15723538 source Swiss-Prot : SWS_FT_FI1 32) chain A residue 159 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_01939, ECO:0000269|PubMed:15723538 source Swiss-Prot : SWS_FT_FI1 33) chain A residue 189 type BINDING sequence A description BINDING => ECO:0000255|HAMAP-Rule:MF_01939, ECO:0000269|PubMed:15723538 source Swiss-Prot : SWS_FT_FI1 34) chain A residue 211 type BINDING sequence I description BINDING => ECO:0000255|HAMAP-Rule:MF_01939, ECO:0000269|PubMed:15723538 source Swiss-Prot : SWS_FT_FI1 35) chain A residue 242 type BINDING sequence A description BINDING => ECO:0000255|HAMAP-Rule:MF_01939, ECO:0000269|PubMed:15723538 source Swiss-Prot : SWS_FT_FI1 36) chain A residue 271 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_01939, ECO:0000269|PubMed:15723538 source Swiss-Prot : SWS_FT_FI1 37) chain B residue 46 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_01939, ECO:0000269|PubMed:15723538 source Swiss-Prot : SWS_FT_FI1 38) chain B residue 124 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_01939, ECO:0000269|PubMed:15723538 source Swiss-Prot : SWS_FT_FI1 39) chain A residue 121-126 type prosite sequence KRCGHR description ISOCITRATE_LYASE Isocitrate lyase signature. KRCGHR source prosite : PS00161 40) chain A residue 86 type BINDING sequence A description BINDING => ECO:0000255|HAMAP-Rule:MF_01939, ECO:0000269|PubMed:12706720, ECO:0000269|PubMed:15723538 source Swiss-Prot : SWS_FT_FI2 41) chain A residue 88 type BINDING sequence I description BINDING => ECO:0000255|HAMAP-Rule:MF_01939, ECO:0000269|PubMed:12706720, ECO:0000269|PubMed:15723538 source Swiss-Prot : SWS_FT_FI2 42) chain B residue 86 type BINDING sequence A description BINDING => ECO:0000255|HAMAP-Rule:MF_01939, ECO:0000269|PubMed:12706720, ECO:0000269|PubMed:15723538 source Swiss-Prot : SWS_FT_FI2 43) chain B residue 88 type BINDING sequence I description BINDING => ECO:0000255|HAMAP-Rule:MF_01939, ECO:0000269|PubMed:12706720, ECO:0000269|PubMed:15723538 source Swiss-Prot : SWS_FT_FI2

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