Structure of PDB 6udo Chain D

Receptor sequence

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

YVPDDGLTAQQLFNCGDGLTYNDFLILPGYIDFTADQVDLTSALTKKITL
KTPLVSSPMDTVTEAGMAIAMALTGGIGFIHHNCTPEFQANEVRKVKKYE
QGFITDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRMGSRLVGIISSR
DIDFLKEEEHDCFLEEIMTKREDLVVAPAGITLKEANEILQRSKKGKLPI
VNEDDELVAIIARTDLKKNRDYPLASKDAKKQLLCGAAIGTHEDDKYRLD
LLAQAGVDVVVLDSSQGNSIFQINMIKYIKDKYPNLQVIGGNVVTAAQAK
NLIDAGVDALRVGMGSGSICITQEVLACGRPQATAVYKVSEYARRFGVPV
IADGGIQNVGHIAKALALGASTVMMGSLLAATTEAPGEYFFSDGIRLKKY
RGMGSLDAMIKVAQGVSGAVQDKGSIHKFVPYLIAGIQHSCQDIGAKSLT
QVRAMMYSGELKFEKRTSSAQVEGGVHSLHSYEKRLF

3D structure

PDB

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

Chain

Resolution

3.21 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	T52 K57 T477 R480	T41 K46 T450 R453
BS02	IMP	D	S68 M70 R322 G328 S329 I330 C331 D364 G365 G387 S388 M414 G415 Q441	S57 M59 R311 G317 S318 I319 C320 D353 G354 G376 S377 M403 G404 Q414
BS03	GTP	D	I115 P118 F139 C140 G141 S159 S160 K208 A223 T225	I104 P107 F128 C129 G130 S148 S149 K197 A212 T214
BS04	GTP	D	L194 K195 N198 D226 L227 N230 K242	L183 K184 N187 D215 L216 N219 K231
BS05	ATP	D	S159 S160 R161 D162 L185 V186 K206 K208	S148 S149 R150 D151 L174 V175 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:6udo, PDBe:6udo, PDBj:6udo
PDBsum	6udo
PubMed	31999252
UniProt	P12268\|IMDH2_HUMAN Inosine-5'-monophosphate dehydrogenase 2 (Gene Name=IMPDH2)

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