Structure of PDB 1pl0 Chain D

Receptor sequence
>1pl0D (length=579) Species: 9606 (Homo sapiens) [Search protein sequence]
GQLALFSVSDKTGLVEFARNLTALGLNLVASGGTAKALRDAGLAVRDVSE
LTGFPEMLGGRVKTLHPAVHAGILARNIPEDNADMARLDFNLIRVVACNL
YPFVKTVASPGVTVEEAVEQIDIGGVTLLRAAAKNHARVTVVCEPEDYVV
VSTEMQSSESKDTSLETRRQLALKAFTHTAQYDEAISDYFRKQYSKGVSQ
MPLRYGMNPHQTPAQLYTLQPKLPITVLNGAPGFINLCDALNAWQLVKEL
KEALGIPAAASFKHVSPAGAAVGIPLSEDEAKVCMVYDLYKTLTPISAAY
ARARGADRMSSFGDFVALSDVCDVPTAKIISREVSDGIIAPGYEEEALTI
LSKKKNGNYCVLQMDQSYKPDENEVRTLFGLHLSQKRNNGVVDKSLFSNV
VTKNKDLPESALRDLIVATIAVKYTQSNSVCYAKNGQVIGIGAGQQSRIH
CTRLAGDKANYWWLRHHPQVLSMISNAIDQYVTGTIGEDEDLIKWKALFE
EVPELLTEAEKKEWVEKLTEVSISSDAFFPFRDNVDRAKRSGVAYIAAPS
GSAADKVVIEACDELGIILAHTNLRLFHH
3D structure
PDB1pl0 Crystal Structures of Human Bifunctional Enzyme Aminoimidazole-4-carboxamide Ribonucleotide Transformylase/IMP Cyclohydrolase in Complex with Potent Sulfonyl-containing Antifolates.
ChainD
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) K263 H264 N428 H579
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 R207 Y208 K266 H267 D339 R204 Y205 K263 H264 D336
BS02 AMZ D N431 R451 A540 F541 R588 F590 N428 R448 A527 F528 R575 F577
BS03 BW2 D N431 S450 R451 I452 P543 F544 D546 N428 S447 R448 I449 P530 F531 D533 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]