Structure of PDB 1sqi Chain B

Receptor sequence
>1sqiB (length=342) Species: 10116 (Rattus norvegicus) [Search protein sequence]
KGPKPERGRFLHFHSVTFWVGNAKQAASFYCNKMGFEPLAYKGLETGSRE
VVSHVIKQGKIVFVLCSALNPWNKEMGDHLVKHGDGVKDIAFEVEDCEHI
VQKARERGAKIVREPWVEEDKFGKVKFAVLQTYGDTTHTLVEKINYTGRF
LPGFEAPTYKDTLLPKLPSCNLEIIDHIVGNQPDQEMESASEWYLKNLQF
HRFWLRSIVVANYEESIKMPINEPASQIQEYVDYNGGAGVQHIALRTEDI
ITTIRHLRERGMEFLAVPSSYYRLLRENLKTSKIQVKENMDVLEELKILV
DYDEKGYLLQIFTKPMQDRPTLFLEVIQRHNHQGFGAGNFNS
3D structure
PDB1sqi Structural basis for herbicidal inhibitor selectivity revealed by comparison of crystal structures of plant and Mammalian 4-hydroxyphenylpyruvate dioxygenases
ChainB
Resolution2.15 Å
3D
structure
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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 B H183 H266 E349 H177 H242 E325
BS02 869 B P239 N241 Q251 H266 L323 F336 F347 E349 F359 N363 F364 P220 N222 Q227 H242 L299 F312 F323 E325 F335 N339 F340 MOAD: ic50<20nM
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:0042803 protein homodimerization activity
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:0000139 Golgi membrane
GO:0005737 cytoplasm
GO:0005783 endoplasmic reticulum
GO:0005789 endoplasmic reticulum membrane
GO:0005794 Golgi apparatus
GO:0016020 membrane

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Cellular Component
External links
PDB RCSB:1sqi, PDBe:1sqi, PDBj:1sqi
PDBsum1sqi
PubMed15301540
UniProtP32755|HPPD_RAT 4-hydroxyphenylpyruvate dioxygenase (Gene Name=Hpd)

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