Structure of PDB 6u9o Chain D

Receptor sequence

>6u9oD (length=488) Species: 9606 (Homo sapiens) [Search protein sequence]

SYVPDDGLTAQQLFNCGDGLTYNDFLILPGYIDFTADQVDLTSALTKKIT
LKTPLVSSPMDTVTEAGMAIAMALTGGIGFIHHNCTPEFQANEVRKVKKY
EQGFITDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRMGSRLVGIISS
RDIDFLKEEEHDCFLEEIMTKREDLVVAPAGITLKEANEILQRSKKGKLP
IVNEDDELVAIIARTDLKKNRDYPLASKDAKKQLLCGAAIGTHEDDKYRL
DLLAQAGVDVVVLDSSQGNSIFQINMIKYIKDKYPNLQVIGGNVVTAAQA
KNLIDAGVDALRVGMGSGSICITQEVLACGRPQATAVYKVSEYARRFGVP
VIADGGIQNVGHIAKALALGASTVMMGSLLAATTEAPGEYFFSDGIRLKK
YRGMGSLDAMIKVAQGVSGAVQDKGSIHKFVPYLIAGIQHSCQDIGAKSL
TQVRAMMYSGELKFEKRTSSAQVEGGVHSLHSYEKRLF

3D structure

PDB

6u9o Cryo-EM structures demonstrate human IMPDH2 filament assembly tunes allosteric regulation.

Chain

Resolution

3.36 Å

3D
structure

[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]

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	K57 R355 R480	K47 R345 R454
BS02	GTP	D	P118 F139 C140 G141 K208 T225 D226	P108 F129 C130 G131 K198 T215 D216
BS03	GTP	D	L194 K195 N198 N230 K242	L184 K185 N188 N220 K232
BS04	ATP	D	I157 S159 S160 R161 D162 L185 K206 K208	I147 S149 S150 R151 D152 L175 K196 K198
BS05	IMP	D	S68 M70 G328 S329 I330 C331 D364 G387 S388 Y411 G413 M414 G415 Q441 G442	S58 M60 G318 S319 I320 C321 D354 G377 S378 Y401 G403 M404 G405 Q415 G416
BS06	NAD	D	H93 T252 H253 D274 S276 F282 N303 M414 Q441	H83 T242 H243 D264 S266 F272 N293 M404 Q415

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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component

External links

PDB	RCSB:6u9o, PDBe:6u9o, PDBj:6u9o
PDBsum	6u9o
PubMed	31999252
UniProt	P12268\|IMDH2_HUMAN Inosine-5'-monophosphate dehydrogenase 2 (Gene Name=IMPDH2)

[Back to BioLiP]