Structure of PDB 6l59 Chain B

Receptor sequence
>6l59B (length=331) Species: 9606 (Homo sapiens) [Search protein sequence]
RHTVTMIPGDGIGPELMLHVKSVFRHACVPVDFEEVHVSSNADEEDIRNA
IMAIRRNRVALKGNIETNHNLPPSHKSRNNILRTSLDLYANVIHCKSLPG
VVTRHKDIDILIVRENTEGEYSSLEHESVAGVVESLKIITKAKSLRIAEY
AFKLAQESGRKKVTAVHKANIMKLGDGLFLQCCREVAARYPQITFENMIV
DNTTMQLVSRPQQFDVMVMPNLYGNIVNNVCAGLVGGPGLVAGANYGHVY
AVFETATRNTGKSIANKNIANPTATLLASCMMLDHLKLHSYATSIRKAVL
ASMDNENMHTPDIGGQGTTSEAIQDVIRHIR
3D structure
PDB6l59 Molecular mechanism of the dual regulatory roles of ATP on the alpha gamma heterodimer of human NAD-dependent isocitrate dehydrogenase.
ChainB
Resolution2.254 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y135 K182 D215 N239
Catalytic site (residue number reindexed from 1) Y121 K168 D201 N225
Enzyme Commision number ?
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 ATP B P252 N273 T274 G275 K276 S277 I278 N285 D326 P238 N259 T260 G261 K262 S263 I264 N271 D312
BS02 MG B N78 R272 N64 R258
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004449 isocitrate dehydrogenase (NAD+) activity
GO:0005515 protein binding
GO:0005524 ATP binding
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:0005730 nucleolus
GO:0005739 mitochondrion
GO:0005759 mitochondrial matrix
GO:0045242 isocitrate dehydrogenase complex (NAD+)

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Cellular Component
External links
PDB RCSB:6l59, PDBe:6l59, PDBj:6l59
PDBsum6l59
PubMed32277159
UniProtP51553|IDH3G_HUMAN Isocitrate dehydrogenase [NAD] subunit gamma, mitochondrial (Gene Name=IDH3G)

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