Structure of PDB 1xg3 Chain A

Receptor sequence
>1xg3A (length=288) Species: 562 (Escherichia coli) [Search protein sequence]
SLHSPGKAFRAALTKENPLQIVGTINANHALLAQRAGYQAIYLSGGGVAA
GSLGLPDLGISTLDDVLTDIRRITDVCSLPLLVDADIGFGSSAFNVARTV
KSMIKAGAAGLHIEDQVGAKRSGHRPNKAIVSKEEMVDRIRAAVDAKTDP
DFVIMARTDALAVEGLDAAIERAQAYVEAGAEMLFPEAITELAMYRQFAD
AVQVPILANITEFGATPLFTTDELRSAHVAMALYPLSAFRAMNRAAEHVY
NVLRQEGTQKSVIDTMQTRNELYESINYYQYEEKLDNL
3D structure
PDB1xg3 Crystal Structures of 2-Methylisocitrate Lyase in Complex with Product and with Isocitrate Inhibitor Provide Insight into Lyase Substrate Specificity, Catalysis and Evolution
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y43 S45 G46 G47 D58 D85 D87 H113 E115 K121 S123 G124 H125 R158 E188 N210 T217 L219
Catalytic site (residue number reindexed from 1) Y42 S44 G45 G46 D57 D84 D86 H112 E114 K120 S122 G123 H124 R157 E187 N209 T216 L218
Enzyme Commision number 4.1.3.30: methylisocitrate lyase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 PYR A Y43 S45 G47 D85 R158 P236 Y42 S44 G46 D84 R157 P235
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0016829 lyase activity
GO:0016833 oxo-acid-lyase activity
GO:0046421 methylisocitrate lyase activity
GO:0046872 metal ion binding
Biological Process
GO:0019629 propionate catabolic process, 2-methylcitrate cycle

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Molecular Function
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Biological Process
External links
PDB RCSB:1xg3, PDBe:1xg3, PDBj:1xg3
PDBsum1xg3
PubMed15723538
UniProtP77541|PRPB_ECOLI 2-methylisocitrate lyase (Gene Name=prpB)

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