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Crystal structure of arabidopsis thaliana hppd truncated mutant complexed with ntbc

Analyse Crystal structure of arabidopsis thaliana hppd truncated mutant complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5YWI
Type: protein
Length: 362 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: NTD, CO
Pockets: 4 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	4-hydroxyphenylpyruvate dioxygenase (EC 1.13.11.27)	protein	362	25% helix, 33% strand	P93836

Ligands and binding sites

NTD · 2-{hydroxy[2-nitro-4-(trifluoromethyl) phenyl]methylene}cyclohexane-1,3-dione · ligand · chains A
CO · Cobalt (II) ion · metal · chains A

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

Pockets

4 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	427	0.64	0.78	44	CO, NTD
2	109	0.47	0.79	20	empty
3	84	0.39	0.77	17	empty
4	68	0.35	0.77	12	empty

Compared structures

5YWI · Crystal structure of Arabidopsis thaliana HPPD Truncated mutant complexed with NTBC · the same entry in another collection · chain A against A, TM-score 1.00

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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 5YWI · PDBe 5YWI · UniProt P93836

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