Structure of PDB 1igw Chain C

Receptor sequence

>1igwC (length=416) Species: 562 (Escherichia coli)

KTRTQQIEELQKEWTQPRWEGITRPYSAEDVVKLRGSVNPECTLAQLGAA
KMWRLLHGESKKGYINSLGALTGGQALQQAKAGIEAVYLSGWQVAADANL
AASMYPDQSLYPANSVPAVVERINNTFRRADQIQWSAGIEPGDPRYVDYF
LPIVADAEAGFGGVLNAFELMKAMIEAGAAAVHFEDQLASVKKCGHMGGK
VLVPTQEAIQKLVAARLCADVTGVPTLLVARTDADAADLITSDCDPYDSE
FITGERTSEGFFRTHAGIEQAISRGLAYAPYADLVWCETSTPDLELARRF
AQAIHAKYPGKLLAYNCSPSFNWQKNLDDKTIASFQQQLSDMGYKFQFIT
LAGIHSMWFNMFDLANAYAQGEGMKHYVEKVQQPEFAAAKDGYTFVSHQQ
EVGTGYFDKVTTIIQG

3D structure

• PDB: 1igw The structure and domain organization of Escherichia coli isocitrate lyase.
• Chain: C
• Resolution: 2.1 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Y89 D108 D157 E159 H184 E186 C195 R232 E289 K312 S319 S321
• Catalytic site (residue number reindexed from 1): Y88 D107 D156 E158 H183 E185 C194 R231 E288 K311 S318 S320
• 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	C	S91 G92 W93 D157 R232 T351	S90 G91 W92 D156 R231 T350

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

External links

• PDB: RCSB:1igw, PDBe:1igw, PDBj:1igw
• PDBsum: 1igw
• PubMed: 11526312
• UniProt: P0A9G6|ACEA_ECOLI Isocitrate lyase (Gene Name=aceA)