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4-hydroxyphenylpyruvate dioxygenase

Analyse 4-hydroxyphenylpyruvate dioxygenase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1SP9
Type: protein
Length: 736 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 4-hydroxyphenylpyruvate dioxygenase
EC: 1.13.11.27
UniProt: P93836
Ligands: FE2
Pockets: 5 · best druggability 0.71

Structure

x-ray diffraction · 2 distinct chains · 24% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	4-hydroxyphenylpyruvate dioxygenase (EC 1.13.11.27)	protein	362	23% helix, 34% strand	P93836
B	4-hydroxyphenylpyruvate dioxygenase (EC 1.13.11.27)	protein	374	26% helix, 34% strand	P93836

Ligands and binding sites

FE2 · Fe (II) ion · metal · 2 copies · chains A, B

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

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	470	0.71	0.81	44	FE2
2	590	0.70	0.79	56	FE2
3	132	0.43	0.76	26	empty
4	58	0.42	0.82	17	empty
5	58	0.31	0.76	18	empty

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

1SP9 · 4-Hydroxyphenylpyruvate Dioxygenase · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P93836
Elsewhere: RCSB PDB 1SP9 · PDBe 1SP9 · UniProt P93836

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