Structure of PDB 1tfz Chain A

Receptor sequence

>1tfzA (length=364) Species: 3702 (Arabidopsis thaliana)

NPKSDKFKVKRFHHIEFWCGDATNVARRFSWGLGMRFSAKSDLSTGNMVH
ASYLLTSGDLRFLFTAPYSPSLSAGEIKPTTTASIPSFDHGSCRSFFSSH
GLGVRAVAIEVEDAESAFSISVANGAIPSSPPIVLNEAVTIAEVKLYGDV
VLRYVSYKEFLPGFERVEDASSFPLDYGIRRLDHAVGNVPELGPALTYVA
GFTGFHQFASGLNSAVLASNDEMVLLPINEPVHGKSQIQTYLEHNEGAGL
QHLALMSEDIFRTLREMRKRSSIGGFDFMPSPPPTYYQNLKKRVGDVLSD
DQIKECEELGILVDRDDQGTLLQIFTKPLGDRPTIFIEIIQRVGCMQSGG
CGGFGKGNFSELFK

3D structure

• PDB: 1tfz Structural basis for herbicidal inhibitor selectivity revealed by comparison of crystal structures of plant and Mammalian 4-hydroxyphenylpyruvate dioxygenases
• Chain: A
• Resolution: 1.8 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	FE	A	H205 H287 E373	H184 H252 E338
BS02	869	A	H205 P259 H287 M314 F360 F398 G399 N402 F403	H184 P227 H252 M279 F325 F354 G355 N358 F359	MOAD: ic50=7nM PDBbind-CN: -logKd/Ki=8.15,IC50=7nM

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