Structure of PDB 5uz0 Chain D

Receptor sequence

>5uz0D (length=588) Species: 9606 (Homo sapiens) [Search protein sequence]

GQLALFSVSDKTGLVEFARNLTALGLNLVASGGTAKALRDAGLAVRDVSE
LTGFPEMLGGRVKTLHPAVHAGILARNIPEDNADMARLDFNLIRVVACNL
YPFVKTVASPVTVEEAVEQIDIGGVTLLRAAAKNHARVTVVCEPEDYVVV
STEMQSSESKDTSLETRRQLALKAFTHTAQYDEAISDYFRKQYSKGVSQM
PLRYGMNPHQTPAQLYTLQPKLPITVLNGAPGFINLCDALNAWQLVKELK
EALGIPAAASFKHVSPAGAAVGIPLSEDEAKVCMVYDLYKTLTPISAAYA
RARGADRMSSFGDFVALSDVCDVPTAKIISREVSDGIIAPGYEEEALTIL
SKKKNGNYCVLQMDQSYKPDENEVRTLFGLHLSQKRNNGVVDKSLFSNVV
TKNKDLPESALRDLIVATIAVKYTQSNSVCYAKNGQVIGIGAGQQSRIHC
TRLAGDKANYWWLRHHPQVLSMKFKTGVKRAEISNAIDQYVTGTIGEDED
LIKWKALFEEVPELLTEAEKKEWVEKLTEVSISSDAFFPFRDNVDRAKRS
GVAYIAAPSGSAADKVVIEACDELGIILAHTNLRLFHH

3D structure

PDB

5uz0 Discovery of N-(6-Fluoro-1-oxo-1,2-dihydroisoquinolin-7-yl)-5-[(3R)-3-hydroxypyrrolidin-1-yl]thiophene-2-sulfonamide (LSN 3213128), a Potent and Selective Nonclassical Antifolate Aminoimidazole-4-carboxamide Ribonucleotide Formyltransferase (AICARFT) Inhibitor Effective at Tumor Suppression in a Cancer Xenograft Model.

Chain

Resolution

1.79 Å

3D
structure

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Enzymatic activity

Enzyme Commision number

2.1.2.3: phosphoribosylaminoimidazolecarboxamide formyltransferase.
3.5.4.10: IMP cyclohydrolase.

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	AMZ	D	Y208 I238 H267 G316 D339	Y204 I234 H263 G312 D335
BS02	8US	D	K266 M312 S313 F315 D339 N489	K262 M308 S309 F311 D335 N485	MOAD: ic50=16nM BindingDB: EC50=7.6nM,IC50=16nM
BS03	8US	D	N431 S450 R451 I452 P543 F544 D546 N547	N427 S446 R447 I448 P539 F540 D542 N543	MOAD: ic50=16nM BindingDB: EC50=7.6nM,IC50=16nM
BS04	AMZ	D	R451 A540 F541 R588 F590	R447 A536 F537 R584 F586
BS05	AMZ	D	S10 V11 S12 S34 G36 T37 R64 V65 K66 T67 N102 Y104 D125 G127 G128	S7 V8 S9 S31 G33 T34 R61 V62 K63 T64 N99 Y101 D121 G123 G124
BS06	MG	D	V425 T428 D539 L589 H591	V421 T424 D535 L585 H587

Gene Ontology

	Molecular Function
GO:0003824	catalytic activity
GO:0003937	IMP cyclohydrolase activity
GO:0004643	phosphoribosylaminoimidazolecarboxamide formyltransferase activity
GO:0016740	transferase activity
GO:0016787	hydrolase activity
GO:0042803	protein homodimerization activity
GO:0045296	cadherin binding

	Biological Process
GO:0003360	brainstem development
GO:0006139	nucleobase-containing compound metabolic process
GO:0006164	purine nucleotide biosynthetic process
GO:0006177	GMP biosynthetic process
GO:0006189	'de novo' IMP biosynthetic process
GO:0021549	cerebellum development
GO:0021987	cerebral cortex development
GO:0031100	animal organ regeneration
GO:0044208	'de novo' AMP biosynthetic process
GO:0046452	dihydrofolate metabolic process
GO:0046654	tetrahydrofolate biosynthetic process
GO:0097294	'de novo' XMP biosynthetic process
GO:0098761	cellular response to interleukin-7

	Cellular Component
GO:0005737	cytoplasm
GO:0005829	cytosol
GO:0005886	plasma membrane
GO:0016020	membrane
GO:0070062	extracellular exosome

View graph for
Molecular Function

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Biological Process

View graph for
Cellular Component

External links

PDB	RCSB:5uz0, PDBe:5uz0, PDBj:5uz0
PDBsum	5uz0
PubMed	29072452
UniProt	P31939\|PUR9_HUMAN Bifunctional purine biosynthesis protein ATIC (Gene Name=ATIC)

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