Structure of PDB 1igw Chain D

Receptor sequence
>1igwD (length=405) Species: 562 (Escherichia coli) [Search protein sequence]
KTRTQQIEELQKEWTQPRWEGITRPYSAEDVVKLRGSVNPECTLAQLGAA
KMWRLLHGESKKGYINSLGALTGGQALQQAKAGIEAVYLSGWQVAADANL
AASMYPDQSLYPANSVPAVVERINNTFRRADQIQWSAGIEPGDPRYVDYF
LPIVADAEAGFGGVLNAFELMKAMIEAGAAAVHFEDQLASVGKVLVPTQE
AIQKLVAARLCADVTGVPTLLVARTDADAADLITSDCDPYDSEFITGERT
SEGFFRTHAGIEQAISRGLAYAPYADLVWCETSTPDLELARRFAQAIHAK
YPGKLLAYNCSPSFNWDDKTIASFQQQLSDMGYKFQFITLAGIHSMWFNM
FDLANAYAQGEGMKHYVEKVQQPEFAAAKDGYTFVSHQQEVGTGYFDKVT
TIIQG
3D structure
PDB1igw The structure and domain organization of Escherichia coli isocitrate lyase.
ChainD
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y89 D108 D157 E159 H184 E186 R232 E289 K312 S319 S321
Catalytic site (residue number reindexed from 1) Y88 D107 D156 E158 H183 E185 R224 E281 K304 S311 S313
Enzyme Commision number 4.1.3.1: isocitrate 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 D S91 G92 W93 D157 R232 T351 S90 G91 W92 D156 R224 T339
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004451 isocitrate lyase activity
GO:0016829 lyase activity
GO:0043169 cation binding
GO:0046872 metal ion binding
Biological Process
GO:0006097 glyoxylate cycle
GO:0006099 tricarboxylic acid cycle
GO:0019752 carboxylic acid metabolic process
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1igw, PDBe:1igw, PDBj:1igw
PDBsum1igw
PubMed11526312
UniProtP0A9G6|ACEA_ECOLI Isocitrate lyase (Gene Name=aceA)

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