Structure of PDB 1tg5 Chain A

Receptor sequence

>1tg5A (length=371) Species: 3702 (Arabidopsis thaliana)

KNPKSDKFKVKRFHHIEFWCGDATNVARRFSWGLGMRFSAKSDLSTGNMV
HASYLLTSGDLRFLFTAPYSPSLSAGEIKPTTTASIPSFDHGSCRSFFSS
HGLGVRAVAIEVEDAESAFSISVANGAIPSSPPIVLNEAVTIAEVKLYGD
VVLRYVSYKASEFLPGFERVEDASSFPLDYGIRRLDHAVGNVPELGPALT
YVAGFTGFHQFAESGLNSAVLASNDEMVLLPINEPVHGTKSQIQTYLEHN
EGAGLQHLALMSEDIFRTLREMRKRSSIGGFDFMPSPPPTYYQNLKKRVG
DVLSDDQIKECEELGILVDRDDQGTLLQIFTKPLGDRPTIFIEIIQRVGC
YQSGGCGGFGKGNFSELFKSI

3D structure

• PDB: 1tg5 Structural basis for herbicidal inhibitor selectivity revealed by comparison of crystal structures of plant and Mammalian 4-hydroxyphenylpyruvate dioxygenases
• Chain: A
• Resolution: 1.9 Å

Enzymatic activity

• Enzyme Commision number: 1.13.11.27: 4-hydroxyphenylpyruvate dioxygenase.

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	FE2	A	H205 H287 E373	H187 H257 E343
BS02	645	A	L244 P259 H287 F360 F371 E373 F398 G399 K400 N402 F403 L406	L216 P231 H257 F330 F341 E343 F359 G360 K361 N363 F364 L367	MOAD: ic50=12nM PDBbind-CN: -logKd/Ki=7.92,IC50=12nM

Gene Ontology

Molecular Function

• GO:0003868 4-hydroxyphenylpyruvate dioxygenase activity
• GO:0005506 iron ion binding
• GO:0016701 oxidoreductase activity, acting on single donors with incorporation of molecular oxygen
• GO:0042802 identical protein binding
• GO:0046872 metal ion binding
• GO:0051213 dioxygenase activity

Biological Process

• GO:0006559 L-phenylalanine catabolic process
• GO:0006572 tyrosine catabolic process
• GO:0009072 aromatic amino acid metabolic process

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:1tg5, PDBe:1tg5, PDBj:1tg5
• PDBsum: 1tg5
• PubMed: 15301540
• UniProt: P93836|HPPD_ARATH 4-hydroxyphenylpyruvate dioxygenase (Gene Name=HPD)