eF-site ID 1mum-A PDB Code 1mum Chain A 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 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 A residue 44 type catalytic sequence L description 182 source MCSA : MCSA1 4) chain A residue 211 type catalytic sequence I description 182 source MCSA : MCSA1 5) chain A residue 59 type catalytic sequence L description 182 source MCSA : MCSA1 6) chain A residue 86 type catalytic sequence A description 182 source MCSA : MCSA1 7) chain A residue 88 type catalytic sequence I description 182 source MCSA : MCSA1 8) chain A residue 114 type catalytic sequence I description 182 source MCSA : MCSA1 9) chain A residue 116 type catalytic sequence D description 182 source MCSA : MCSA1 10) chain A residue 124 type catalytic sequence G description 182 source MCSA : MCSA1 11) chain A residue 159 type catalytic sequence T description 182 source MCSA : MCSA1 12) chain A residue 189 type catalytic sequence A description 182 source MCSA : MCSA1 13) chain A residue 121-126 type prosite sequence KRCGHR description ISOCITRATE_LYASE Isocitrate lyase signature. KRCGHR source prosite : PS00161 14) 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 15) 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 16) 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 17) 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 18) 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 19) 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 20) 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 21) 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 22) 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

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