Structure of PDB 6udq Chain C

Receptor sequence

>6udqC (length=487) Species: 9606 (Homo sapiens) [Search protein sequence]

YVPDDGLTAQQLFNCGDGLTYNDFLILPGYIDFTADQVDLTSALTKKITL
KTPLVSSPMDTVTEAGMAIAMALTGGIGFIHHNCTPEFQANEVRKVKKYE
QGFITDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRMGSRLVGIISSR
DIDFLKEEEHDCFLEEIMTKREDLVVAPAGITLKEANEILQRSKKGKLPI
VNEDDELVAIIARTDLKKNRDYPLASKDAKKQLLCGAAIGTHEDDKYRLD
LLAQAGVDVVVLDSSQGNSIFQINMIKYIKDKYPNLQVIGGNVVTAAQAK
NLIDAGVDALRVGMGSGSICITQEVLACGRPQATAVYKVSEYARRFGVPV
IADGGIQNVGHIAKALALGASTVMMGSLLAATTEAPGEYFFSDGIRLKKY
RGMGSLDAMIKVAQGVSGAVQDKGSIHKFVPYLIAGIQHSCQDIGAKSLT
QVRAMMYSGELKFEKRTSSAQVEGGVHSLHSYEKRLF

3D structure

PDB

6udq Cryo-EM structures demonstrate human IMPDH2 filament assembly tunes allosteric regulation.

Chain

Resolution

3.27 Å

3D
structure

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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)
BS01	peptide	C	T52 S53 E352 R355 R356 T477 R480	T41 S42 E341 R344 R345 T450 R453
BS02	IMP	C	M70 R322 G328 S329 I330 C331 D364 G365 G387 S388 Y411 G413 M414 G415 Q441	M59 R311 G317 S318 I319 C320 D353 G354 G376 S377 Y400 G402 M403 G404 Q414
BS03	GTP	C	P118 F139 C140 G141 S160 K208 T225 D226	P107 F128 C129 G130 S149 K197 T214 D215
BS04	GTP	C	Q112 G113 L194 N198 N230 K242	Q101 G102 L183 N187 N219 K231
BS05	ATP	C	S159 S160 R161 D162 T180 L185 K206 K208	S148 S149 R150 D151 T169 L174 K195 K197

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

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Molecular Function

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Cellular Component

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)

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