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Structural basis for inhibitor selectivity revealed by crystal structures of plant and mammalian 4-hydroxyphenylpyruvate dioxygenases

Analyse Structural basis for inhibitor selectivity revealed by crystal structures of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1SQD
Type: protein
Length: 373 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 4-hydroxyphenylpyruvate dioxygenase
EC: 1.13.11.27
UniProt: P93836
Ligands: FE
Pockets: 3 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	4-hydroxyphenylpyruvate dioxygenase (EC 1.13.11.27)	protein	373	28% helix, 35% strand	P93836

Ligands and binding sites

FE · Fe (III) ion · metal · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	429	0.72	0.82	41	empty
2	68	0.37	0.78	14	empty
3	70	0.35	0.77	13	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

1SQD · Structural basis for inhibitor selectivity revealed by crystal structures of plant and… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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Every structure of UniProt P93836
Elsewhere: RCSB PDB 1SQD · PDBe 1SQD · UniProt P93836

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