Structure of PDB 6udq Chain H

Receptor sequence

>6udqH (length=488) Species: 9606 (Homo sapiens)

SYVPDDGLTAQQLFNCGDGLTYNDFLILPGYIDFTADQVDLTSALTKKIT
LKTPLVSSPMDTVTEAGMAIAMALTGGIGFIHHNCTPEFQANEVRKVKKY
EQGFITDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRMGSRLVGIISS
RDIDFLKEEEHDCFLEEIMTKREDLVVAPAGITLKEANEILQRSKKGKLP
IVNEDDELVAIIARTDLKKNRDYPLASKDAKKQLLCGAAIGTHEDDKYRL
DLLAQAGVDVVVLDSSQGNSIFQINMIKYIKDKYPNLQVIGGNVVTAAQA
KNLIDAGVDALRVGMGSGSICITQEVLACGRPQATAVYKVSEYARRFGVP
VIADGGIQNVGHIAKALALGASTVMMGSLLAATTEAPGEYFFSDGIRLKK
YRGMGSLDAMIKVAQGVSGAVQDKGSIHKFVPYLIAGIQHSCQDIGAKSL
TQVRAMMYSGELKFEKRTSSAQVEGGVHSLHSYEKRLF

3D structure

• PDB: 6udq Cryo-EM structures demonstrate human IMPDH2 filament assembly tunes allosteric regulation.
• Chain: H
• Resolution: 3.27 Å

Enzymatic activity

• Enzyme Commision number: 1.1.1.205: IMP dehydrogenase.

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	IMP	H	M70 G328 S329 I330 C331 D364 G365 G387 S388 M414 G415 Q441 G442	M60 G318 S319 I320 C321 D354 G355 G377 S378 M404 G405 Q415 G416
BS02	GTP	H	I115 F139 G141 K208 T225 D226	I105 F129 G131 K198 T215 D216
BS03	GTP	H	E111 Q112 L194 N198 L227 N230 K242	E101 Q102 L184 N188 L217 N220 K232
BS04	ATP	H	S159 S160 R161 D162 T180 L185 K206 K208	S149 S150 R151 D152 T170 L175 K196 K198

Gene Ontology

Molecular Function

• GO:0000166 nucleotide binding
• GO:0003677 DNA binding
• GO:0003723 RNA binding
• GO:0003824 catalytic activity
• GO:0003938 IMP dehydrogenase activity
• GO:0005515 protein binding
• GO:0016491 oxidoreductase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0006164 purine nucleotide biosynthetic process
• GO:0006177 GMP biosynthetic process
• GO:0006183 GTP biosynthetic process
• GO:0007623 circadian rhythm
• GO:0046651 lymphocyte proliferation
• GO:0071353 cellular response to interleukin-4
• GO:0097294 'de novo' XMP biosynthetic process

Cellular Component

• GO:0005576 extracellular region
• GO:0005634 nucleus
• GO:0005737 cytoplasm
• GO:0005778 peroxisomal membrane
• GO:0005829 cytosol
• GO:0016020 membrane
• GO:0034774 secretory granule lumen
• GO:0070062 extracellular exosome
• GO:1904813 ficolin-1-rich granule lumen

External links

• PDB: RCSB:6udq, PDBe:6udq, PDBj:6udq
• PDBsum: 6udq
• PubMed: 31999252
• UniProt: P12268|IMDH2_HUMAN Inosine-5'-monophosphate dehydrogenase 2 (Gene Name=IMPDH2)