Structure of PDB 3blw Chain J

Receptor sequence
>3blwJ (length=347) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
KQPSIGRYTGKPNPSTGKYTVSFIEGDGIGPEISKSVKKIFSAANVPIEW
ESCDVSPIFVNGLTTIPDPAVQSITKNLVALKGPLATPHRSLNLTLRKTF
GLFANVRPAKSIEGFKTTYENVDLVLIRENTEGEYSGIEHIVCPGVVQSI
KLITRDASERVIRYAFEYARAIGRPRVIVVHKSTIQRLADGLFVNVAKEL
SKEYPDLTLETELIDNSVLKVVTNPSAYTDAVSVCPNLYGDILSDLNSGL
SAGSLGLTPSANIGHKISIFEAVHGSAPDIAGQDKANPTALLLSSVMMLN
HMGLTNHADQIQNAVLSTIASGPENRTGDLAGTATTSSFTEAVIKRL
3D structure
PDB3blw Allosteric Motions in Structures of Yeast NAD+-specific Isocitrate Dehydrogenase.
ChainJ
Resolution4.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y142 K189 D222 D248 D252
Catalytic site (residue number reindexed from 1) Y135 K182 D215 D241 D245
Enzyme Commision number 1.1.1.41: isocitrate dehydrogenase (NAD(+)).
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 FLC J K189 T191 K182 T184
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003723 RNA binding
GO:0004449 isocitrate dehydrogenase (NAD+) 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:0006099 tricarboxylic acid cycle
GO:0006102 isocitrate metabolic process
GO:0006537 glutamate biosynthetic process
Cellular Component
GO:0005739 mitochondrion
GO:0005759 mitochondrial matrix
GO:0045242 isocitrate dehydrogenase complex (NAD+)

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:3blw, PDBe:3blw, PDBj:3blw
PDBsum3blw
PubMed18256028
UniProtP28241|IDH2_YEAST Isocitrate dehydrogenase [NAD] subunit 2, mitochondrial (Gene Name=IDH2)

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