Structure of PDB 1m9n Chain B

Receptor sequence
>1m9nB (length=590) Species: 9031 (Gallus gallus) [Search protein sequence]
RQQLALLSVSEKAGLVEFARSLNALGLGLIASGGTATALRDAGLPVRDVS
DLTGFPEMLGGRVKTLHPAVHAGILARNIPEDNADMNKQDFSLVRVVVCN
LYPFVKTVSSPGVTVPEAVEKIDIGGVALLRAAAKNHARVTVVCDPADYS
SVAKEMAASKDKDTSVETRRHLALKAFTHTAQYDAAISDYFRKEYSKGVS
QLPLRYGMNPHQSPAQLYTTRPKLPLTVVNGSPGFINLCDALNAWQLVKE
LKQALGIPAAASFKHVSPAGAAVGIPLSEEEAQVCMVHDLHKTLTPLASA
YARSRGADRMSSFGDFIALSDICDVPTAKIISREVSDGVVAPGYEEEALK
ILSKKKNGGYCVLQMDPNYEPDDNEIRTLYGLQLMQKRNNAVIDRSLFKN
IVTKNKTLPESAVRDLIVASIAVKYTQSNSVCYAKDGQVIGIGAGQQSRI
HCTRLAGDKANSWWLRHHPRVLSMKFKAGVKRAEVSNAIDQYVTGTIGED
EDLVKWQAMFEEVPAQLTEAEKKQWIAKLTAVSLSSDAFFPFRDNVDRAK
RIGVQFIVAPSGSAADEVVIEACNELGITLIHTNLRLFHH
3D structure
PDB1m9n Structural Insights into the Avian AICAR Transformylase Mechanism.
ChainB
Resolution1.93 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K267 H268 N432 H593
Catalytic site (residue number reindexed from 1) K264 H265 N429 H590
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 B A541 F542 R589 F591 A538 F539 R586 F588
BS02 AMZ B Y209 I239 K267 H268 G317 D340 Y206 I236 K264 H265 G314 D337
BS03 XMP B S11 V12 S13 S35 G37 T38 R65 K67 T68 N103 L104 Y105 D126 G128 G129 S8 V9 S10 S32 G34 T35 R62 K64 T65 N100 L101 Y102 D123 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
Biological Process
GO:0006164 purine nucleotide biosynthetic process
GO:0006189 'de novo' IMP biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1m9n, PDBe:1m9n, PDBj:1m9n
PDBsum1m9n
PubMed12501179
UniProtP31335|PUR9_CHICK Bifunctional purine biosynthesis protein ATIC (Gene Name=ATIC)

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