Structure of PDB 1oz0 Chain B

Receptor sequence
>1oz0B (length=590) Species: 9031 (Gallus gallus) [Search protein sequence]
RQQLALLSVSEKAGLVEFARSLNALGLGLIASGGTATALRDAGLPVRDVS
DLTGFPEMLGGRVKTLHPAVHAGILARNIPEDNADMNKQDFSLVRVVVCN
LYPFVKTVSSPGVTVPEAVEKIDIGGVALLRAAAKNHARVTVVCDPADYS
SVAKEMAASKDKDTSVETRRHLALKAFTHTAQYDAAISDYFRKEYSKGVS
QLPLRYGMNPHQSPAQLYTTRPKLPLTVVNGSPGFINLCDALNAWQLVKE
LKQALGIPAAASFKHVSPAGAAVGIPLSEEEAQVCMVHDLHKTLTPLASA
YARSRGADRMSSFGDFIALSDICDVPTAKIISREVSDGVVAPGYEEEALK
ILSKKKNGGYCVLQMDPNYEPDDNEIRTLYGLQLMQKRNNAVIDRSLFKN
IVTKNKTLPESAVRDLIVASIAVKYTQSNSVCYAKDGQVIGIGAGQQSRI
HCTRLAGDKANSWWLRHHPRVLSMKFKAGVKRAEVSNAIDQYVTGTIGED
EDLVKWQAMFEEVPAQLTEAEKKQWIAKLTAVSLSSDAFFPFRDNVDRAK
RIGVQFIVAPSGSAADEVVIEACNELGITLIHTNLRLFHH
3D structure
PDB1oz0 Structure of Avian AICAR Transformylase with a Multisubstrate Adduct Inhibitor beta-DADF Identifies the Folate Binding Site.
ChainB
Resolution2.5 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 MS1 B Y209 I239 K267 M313 F316 G317 D340 Y206 I236 K264 M310 F313 G314 D337 MOAD: Kd=20nM
PDBbind-CN: -logKd/Ki=7.70,Kd=20nM
BS02 PO4 B G36 G37 T38 K67 G33 G34 T35 K64
BS03 MS1 B Q450 S451 R452 I453 A541 F542 P544 F545 S566 A567 R589 F591 Q447 S448 R449 I450 A538 F539 P541 F542 S563 A564 R586 F588 MOAD: Kd=20nM
PDBbind-CN: -logKd/Ki=7.70,Kd=20nM
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:1oz0, PDBe:1oz0, PDBj:1oz0
PDBsum1oz0
PubMed12974624
UniProtP31335|PUR9_CHICK Bifunctional purine biosynthesis protein ATIC (Gene Name=ATIC)

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