Structure of PDB 1igw Chain A

Receptor sequence
>1igwA (length=396) Species: 562 (Escherichia coli) [Search protein sequence]
KTRTQQIEELQKEWTQPRWEGITRPYSAEDVVKLRGSVNPECTLAQLGAA
KMWRLLHGESKKGYINSLGALTGGQALQQAKAGIEAVYLSGWQVAADANL
AASMYPDQSLYPANSVPAVVERINNTFRRADQIQWSAGIEPGDPRYVDYF
LPIVADAEAGFGGVLNAFELMKAMIEAGAAAVHFEDQLASVKKCGKVLVP
TQEAIQKLVAARLCADVTGVPTLLVARTDADAADLITSDCDPYDSEFITG
ERTSEGFFRTHAGIEQAISRGLAYAPYADLVWCETSTPDLELARRFAQAI
HAKYPGKLLAYNCSFQQQLSDMGYKFQFITLAGIHSMWFNMFDLANAYAQ
GEGMKHYVEKVQQPEFAAAKDGYTFVSHQQEVGTGYFDKVTTIIQG
3D structure
PDB1igw The structure and domain organization of Escherichia coli isocitrate lyase.
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) Y89 D108 D157 E159 H184 E186 C195 R232 E289 K312
Catalytic site (residue number reindexed from 1) Y88 D107 D156 E158 H183 E185 C194 R227 E284 K307
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 A S91 W93 D157 R232 T351 S90 W92 D156 R227 T330
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

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

[Back to BioLiP]