Structure of PDB 5grl Chain A

Receptor sequence

>5grlA (length=323) Species: 9606 (Homo sapiens)

VQTVTLIPGDGIGPEISAAVMKIFDAAKAPIQWEERNVTAIQWMIPSEAK
ESMDKNKMGLKGPLKTPSMNLLLRKTFDLYANVRPCVSIEGYKTPYTDVN
IVTIRENTEGEYSGIEHVIVDGVVQSIKLITEGASKRIAEFAFEYARNNH
RSNVTAVHKANIMRMSDGLFLQKCREVAESCKDIKFNEMYLDTVCLNMVQ
DPSQFDVLVMPNLYGDILSDLCAGLIGGLGVTPSGNIGANGVAIFESVHG
TAPDIAGKDMANPTALLLSAVMMLRHMGLFDHAARIEAACFATIKDGKSL
TKDGGNAKCSDFTEEICRRVKDL

3D structure

• PDB: 5grl Molecular mechanism of the allosteric regulation of the alpha gamma heterodimer of human NAD-dependent isocitrate dehydrogenase.
• Chain: A
• Resolution: 2.79 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Y126 K173 D206 D230 D234
• Catalytic site (residue number reindexed from 1): Y112 K159 D192 D216 D220
• 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	MG	A	D230 D234	D216 D220

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion 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:0005975 carbohydrate metabolic process
• GO:0006099 tricarboxylic acid cycle
• GO:0006102 isocitrate metabolic process

Cellular Component

• GO:0005634 nucleus
• GO:0005739 mitochondrion
• GO:0005759 mitochondrial matrix
• GO:0045242 isocitrate dehydrogenase complex (NAD+)

External links

• PDB: RCSB:5grl, PDBe:5grl, PDBj:5grl
• PDBsum: 5grl
• PubMed: 28098230
• UniProt: P50213|IDH3A_HUMAN Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial (Gene Name=IDH3A)