Structure of PDB 5e9f Chain D

Receptor sequence
>5e9fD (length=453) Species: 242507 (Pyricularia oryzae 70-15) [Search protein sequence]
MVNPAVEPSMEDDLFAREVAEVKQWWSDPRWRYTKRPFTAEQIVSKRGNL
KIEYPSNAQSKKLWKILEGRFQKRDASYTYGCLEPTMVTQMAKYLDTVYV
SGWQSSSTASSSDEPGPDLADYPYTTVPNKVSHLFMAQLFHDRKQRHERL
SAPKSERSKLQNIDYLRPIIADADTGHGGLTAVMKLTKLFIEKGAAGIHI
EDQAPGTGKVLVPISEHINRLVAIRAQADIMGVDLLAIARTDAEAATLIT
TSIDPRDHAFILGCTNPSLQLKRFDGKSNREARAIASSLGFFDWDSPRTR
EGYFRIKGGCDCAINRAIAYAPYADAIWMESKLPDYEQAKEFAEGVHAVY
PEQKLAYNLSPSFNWKTAMPRDEQETYIRRLAGLGYCWQFITLAGLHTTA
LISDRFARAYSEVGMRAYGELVQEPEMELGVDVVKHQKWSGATYVDELQK
MVT
3D structure
PDB5e9f Crystal structure and functional analysis of isocitrate lyases from Magnaporthe oryzae and Fusarium graminearum
ChainD
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y104 D123 D177 D179 H204 E206 R252 E405 Q428 S435 S437
Catalytic site (residue number reindexed from 1) Y99 D118 D172 D174 H199 E201 R240 E330 Q353 S360 S362
Enzyme Commision number 4.1.3.1: isocitrate lyase.
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 MG D D123 D177 D118 D172
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004451 isocitrate lyase activity
GO:0016829 lyase activity
GO:0046421 methylisocitrate lyase activity
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:0005737 cytoplasm
GO:0009514 glyoxysome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5e9f, PDBe:5e9f, PDBj:5e9f
PDBsum5e9f
PubMed27016285
UniProtP0CT06|ACEA_PYRO7 Isocitrate lyase (Gene Name=ICL1)

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