MolNFT v2 · #212661 · protein

Crystal structure of AtHPPD-YH20282 complex

8I2U · 4-hydroxyphenylpyruvate dioxygenase: “Crystal structure of AtHPPD-YH20282 complex”. X-ray diffraction at 1.989, 2 ligands (T5I, CO), 2 pockets (best druggability 0.68). MolNFT v2 #212661 on GenesisL1: 3D structure, binding sites and…

PDB: 8I2U
Type: protein
Length: 381 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.989
Source: Arabidopsis thaliana
Molecule: 4-hydroxyphenylpyruvate dioxygenase
EC: 1.13.11.27
UniProt: P93836
Ligands: T5I, CO
Pockets: 2 · best druggability 0.68

Structure

x-ray diffraction · resolution 1.989 · 1 distinct chain · 29% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	4-hydroxyphenylpyruvate dioxygenase (EC 1.13.11.27)	protein	381	29% helix, 33% strand	P93836

Ligands and binding sites

T5I · 2-[2-chloranyl-4-methylsulfonyl-3-(2-trimethylsilylethoxy)phenyl]carbonyl-3-oxidanyl-cyclohex-2-en-1-one · 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

2 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	403	0.68	0.80	43	T5I
2	67	0.34	0.77	12	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

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 8I2U · PDBe 8I2U · UniProt P93836

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