Structure of PDB 2qfy Chain C

Receptor sequence
>2qfyC (length=411) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
AFSKIKVKQPVVELDGDEMTRIIWDKIKKKLILPYLDVDLKYYDLSVESR
DATSDKITQDAAEAIKKYGVGIKCATITPDEARVKEFNLHKMWKSPNGTI
RNILGGTVFREPIVIPRIPRLVPRWEKPIIIGRHAHGDQYKATDTLIPGP
GSLELVYKPSDPTTAQPQTLKVYDYKGSGVAMAMYNTDESIEGFAHSSFK
LAIDKKLNLFLSTKNTILKKYDGRFKDIFQEVYEAQYKSKFEQLGIHYEH
RLIDDMVAQMIKSKGGFIMALKNYDGDVQSDIVAQGFGSLGLMTSILVTP
DGKTFESEAAHGTVTRHYRKYQKGEETSTNSIASIFAWSRGLLKRGELDN
TPALCKFANILESATLNTVQQDGIMTKDLALACGNNERSAYVTTEEFLDA
VEKRLQKEIKS
3D structure
PDB2qfy Structural studies of Saccharomyces cerevesiae mitochondrial NADP-dependent isocitrate dehydrogenase in different enzymatic states reveal substantial conformational changes during the catalytic reaction
ChainC
Resolution2.1 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.1.1.42: isocitrate dehydrogenase (NADP(+)).
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 AKG C S95 N97 R101 S95 N97 R101
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004450 isocitrate dehydrogenase (NADP+) activity
GO:0005515 protein binding
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0046872 metal ion binding
GO:0051287 NAD binding
Biological Process
GO:0006097 glyoxylate cycle
GO:0006099 tricarboxylic acid cycle
GO:0006102 isocitrate metabolic process
GO:0006537 glutamate biosynthetic process
GO:0006739 NADP metabolic process
Cellular Component
GO:0005739 mitochondrion
GO:0042645 mitochondrial nucleoid

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2qfy, PDBe:2qfy, PDBj:2qfy
PDBsum2qfy
PubMed18552125
UniProtP21954|IDHP_YEAST Isocitrate dehydrogenase [NADP], mitochondrial (Gene Name=IDP1)

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