eF-site ID 1mum-B PDB Code 1mum Chain 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 B:  LHSPGKAFRAALTKENPLQIVGTINANHALLAQRAGYQAI YLSGGGVAAGSLGLPDLGISTLDDVLTDIRRITDVCSLPL LVDADIGFGSSAFNVARTVKSMIKAGAAGLHIEDQVGAKR CGHRPNKAIVSKEEMVDRIRAAVDAKTDPDFVIMARTDAL AVEGLDAAIERAQAYVEAGAEMLFPEAITELAMYRQFADA VQVPILANITEFGATPLFTTDELRSAHVAMALYPLSAFRA MNRAAEHVYNVLRQEGTQKSVIDTMQTRNELYESINYYQY EEKLDNLFA Description Functional site 1) chain B residue 58 type sequence D description BINDING SITE FOR RESIDUE MG B 1002 source : AC2 2) chain B residue 87 type sequence D description BINDING SITE FOR RESIDUE MG B 1002 source : AC2 3) chain B residue 44 type catalytic sequence L description 182 source MCSA : MCSA2 4) chain B residue 211 type catalytic sequence I description 182 source MCSA : MCSA2 5) chain B residue 59 type catalytic sequence L description 182 source MCSA : MCSA2 6) chain B residue 86 type catalytic sequence A description 182 source MCSA : MCSA2 7) chain B residue 88 type catalytic sequence I description 182 source MCSA : MCSA2 8) chain B residue 114 type catalytic sequence I description 182 source MCSA : MCSA2 9) chain B residue 116 type catalytic sequence D description 182 source MCSA : MCSA2 10) chain B residue 124 type catalytic sequence G description 182 source MCSA : MCSA2 11) chain B residue 159 type catalytic sequence T description 182 source MCSA : MCSA2 12) chain B residue 189 type catalytic sequence A description 182 source MCSA : MCSA2 13) 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 14) 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 15) 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 16) 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 17) 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 18) 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 19) 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 20) 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 21) 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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