Structure of PDB 6udq Chain D

Receptor sequence

>6udqD (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	D	E352 R355 R356 V359 T477 R480	E341 R344 R345 V348 T450 R453
BS02	IMP	D	M70 G328 S329 I330 C331 D364 G365 G387 S388 Y411 G413 M414 G415 Q441	M59 G317 S318 I319 C320 D353 G354 G376 S377 Y400 G402 M403 G404 Q414
BS03	GTP	D	P118 F139 C140 G141 S160 K208 T225 D226	P107 F128 C129 G130 S149 K197 T214 D215
BS04	GTP	D	Q112 G113 L194 K195 N198 N230 K242	Q101 G102 L183 K184 N187 N219 K231
BS05	ATP	D	I157 S159 S160 R161 D162 L185 V186 K206	I146 S148 S149 R150 D151 L174 V175 K195

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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