Structure of PDB 1p4r Chain A

Receptor sequence

>1p4rA (length=589) Species: 9606 (Homo sapiens) [Search protein sequence]

GQLALFSVSDKTGLVEFARNLTALGLNLVASGGTAKALRDAGLAVRDVSE
LTGFPEMLGGRVKTLHPAVHAGILARNIPEDNADMARLDFNLIRVVACNL
YPFVKTVASPGVTVEEAVEQIDIGGVTLLRAAAKNHARVTVVCEPEDYVV
VSTEMQSSESKDTSLETRRQLALKAFTHTAQYDEAISDYFRKQYSKGVSQ
MPLRYGMNPHQTPAQLYTLQPKLPITVLNGAPGFINLCDALNAWQLVKEL
KEALGIPAAASFKHVSPAGAAVGIPLSEDEAKVCMVYDLYKTLTPISAAY
ARARGADRMSSFGDFVALSDVCDVPTAKIISREVSDGIIAPGYEEEALTI
LSKKKNGNYCVLQMDQSYKPDENEVRTLFGLHLSQKRNNGVVDKSLFSNV
VTKNKDLPESALRDLIVATIAVKYTQSNSVCYAKNGQVIGIGAGQQSRIH
CTRLAGDKANYWWLRHHPQVLSMKFKTGVKRAEISNAIDQYVTGTIGEDE
DLIKWKALFEEVPELLTEAEKKEWVEKLTEVSISSDAFFPFRDNVDRAKR
SGVAYIAAPSGSAADKVVIEACDELGIILAHTNLRLFHH

3D structure

PDB

1p4r Crystal structures of human bifunctional enzyme aminoimidazole-4-carboxamide ribonucleotide transformylase/IMP cyclohydrolase in complex with potent sulfonyl-containing antifolates

Chain

Resolution

2.55 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	K266 H267 N431 H592
Catalytic site (residue number reindexed from 1)	K263 H264 N428 H589
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	A	R451 A540 F541 R588 F590	R448 A537 F538 R585 F587
BS02	354	A	Q449 S450 R451 I452 P543 F544 D546 N547 S565 A566	Q446 S447 R448 I449 P540 F541 D543 N544 S562 A563	PDBbind-CN: -logKd/Ki=8.10,Ki=8nM
BS03	XMP	A	S10 V11 S12 S34 G36 T37 R64 K66 T67 N102 L103 Y104 D125 I126 G127 G128	S7 V8 S9 S31 G33 T34 R61 K63 T64 N99 L100 Y101 D122 I123 G124 G125
BS04	AMZ	A	Y208 I238 K266 H267 G316 D339	Y205 I235 K263 H264 G313 D336
BS05	354	A	K266 M312 F315 N489	K263 M309 F312 N486	PDBbind-CN: -logKd/Ki=8.10,Ki=8nM

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

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Cellular Component

External links

PDB	RCSB:1p4r, PDBe:1p4r, PDBj:1p4r
PDBsum	1p4r
PubMed	14966129
UniProt	P31939\|PUR9_HUMAN Bifunctional purine biosynthesis protein ATIC (Gene Name=ATIC)

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