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Crystal structure of athppd-Y18027 complex

Analyse Crystal structure of athppd-Y18027 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7X64
Type: protein
Length: 380 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: 9XU, CO
Pockets: 3 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	4-hydroxyphenylpyruvate dioxygenase (EC 1.13.11.27)	protein	380	31% helix, 33% strand	P93836

Ligands and binding sites

9XU · 1,5-dimethyl-6-(2-oxidanyl-6-oxidanylidene-cyclohexen-1-yl)carbonyl-3-(phenylmethyl)quinazoline-2,4-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

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	509	0.69	0.79	54	9XU
2	60	0.38	0.79	15	empty
3	58	0.34	0.77	12	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

7X64 · Crystal structure of AtHPPD-Y18027 complex · 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 7X64 · PDBe 7X64 · UniProt P93836

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