Structure of PDB 1pl0 Chain C

Receptor sequence
>1pl0C (length=585) Species: 9606 (Homo sapiens) [Search protein sequence]
QLALFSVSDKTGLVEFARNLTALGLNLVASGGTAKALRDAGLAVRDVSEL
TGFPEMLGGRVKTLHPAVHAGILARNIPEDNADMARLDFNLIRVVACNLY
PFVKTVASPGVTVEEAVEQIDIGGVTLLRAAAKNHARVTVVCEPEDYVVV
STEMQSSESKDTSLETRRQLALKAFTHTAQYDEAISDYFRKQYSKGVSQM
PLRYGMNPHQTPAQLYTLQPKLPITVLNGAPGFINLCDALNAWQLVKELK
EALGIPAAASFKHVSPAGAAVGIPLSEDEAKVCMVYDLYKTLTPISAAYA
RARGADRMSSFGDFVALSDVCDVPTAKIISREVSDGIIAPGYEEEALTIL
SKKKNGNYCVLQMDQSYKPDENEVRTLFGLHLSQKRNNGVVDKSLFSNVV
TKNKDLPESALRDLIVATIAVKYTQSNSVCYAKNGQVIGIGAGQQSRIHC
TRLAGDKANYWWLRHHPQVLSMKFKTGAEISNAIDQYVTGTIGEDEDLIK
WKALFEEVPELLTEAEKKEWVEKLTEVSISSDAFFPFRDNVDRAKRSGVA
YIAAPSGSAADKVVIEACDELGIILAHTNLRLFHH
3D structure
PDB1pl0 Crystal Structures of Human Bifunctional Enzyme Aminoimidazole-4-carboxamide Ribonucleotide Transformylase/IMP Cyclohydrolase in Complex with Potent Sulfonyl-containing Antifolates.
ChainC
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the 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
Catalytic site (original residue number in PDB) K266 H267 N431 H592
Catalytic site (residue number reindexed from 1) K262 H263 N427 H585
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 C S10 V11 S34 G36 T37 R64 K66 T67 L68 N102 Y104 D125 G127 S6 V7 S30 G32 T33 R60 K62 T63 L64 N98 Y100 D121 G123
BS02 AMZ C N431 R451 A540 F541 R588 F590 N427 R447 A533 F534 R581 F583
BS03 AMZ C R207 K266 H267 D339 R203 K262 H263 D335
BS04 BW2 C K266 M312 F315 N489 K262 M308 F311 N482 BindingDB: Ki=6.0nM,IC50=1000nM
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
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1pl0, PDBe:1pl0, PDBj:1pl0
PDBsum1pl0
PubMed14966129
UniProtP31939|PUR9_HUMAN Bifunctional purine biosynthesis protein ATIC (Gene Name=ATIC)

[Back to BioLiP]