Structure of PDB 1pkx Chain A

Receptor sequence
>1pkxA (length=588) Species: 9606 (Homo sapiens) [Search protein sequence]
PGQLALFSVSDKTGLVEFARNLTALGLNLVASGGTAKALRDAGLAVRDVS
ELTGFPEMLGGRVKTLHPAVHAGILARNIPEDNADMARLDFNLIRVVACN
LYPFVKTVASPGVTVEEAVEQIDIGGVTLLRAAAKNHARVTVVCEPEDYV
VVSTEMQSSESKDTSLETRRQLALKAFTHTAQYDEAISDYFRKQYSKGVS
QMPLRYGMNPHQTPAQLYTLQPKLPITVLNGAPGFINLCDALNAWQLVKE
LKEALGIPAAASFKHVSPAGAAVGIPLSEDEAKVCMVYDLYKTLTPISAA
YARARGADRMSSFGDFVALSDVCDVPTAKIISREVSDGIIAPGYEEEALT
ILSKKKNGNYCVLQMDQSYKPDENEVRTLFGLHLSQKRNNGVVDKSLFSN
VVTKNKDLPESALRDLIVATIAVKYTQSNSVCYAKNGQVIGIGAGQQSRI
HCTRLAGDKANYWWLRHHPQVLSMKFKTGVAEISNAIDQYVTGTIGEDED
LIKWKALFEEVPELLTEAEKKEWVEKLTEVSISSDAFFPFRDNVDRAKRS
GVAYIAAPSGSAADKVVIEACDELGIILAHTNLRLFHH
3D structure
PDB1pkx Structural Insights into the Human and Avian IMP Cyclohydrolase Mechanism via Crystal Structures with the Bound XMP Inhibitor.
ChainA
Resolution1.9 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) K264 H265 N429 H588
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 XMP A S10 V11 S12 S34 G36 T37 R64 K66 T67 N102 L103 Y104 D125 I126 G127 G128 S8 V9 S10 S32 G34 T35 R62 K64 T65 N100 L101 Y102 D123 I124 G125 G126 MOAD: Ki=0.12uM
PDBbind-CN: -logKd/Ki=6.92,Ki=0.12uM
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1pkx, PDBe:1pkx, PDBj:1pkx
PDBsum1pkx
PubMed14756553
UniProtP31939|PUR9_HUMAN Bifunctional purine biosynthesis protein ATIC (Gene Name=ATIC)

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