MolNFT v1 · #190432 · protein

Crystal structure of athppd-Y14157 complex

7X5S · 4-hydroxyphenylpyruvate dioxygenase: “Crystal structure of athppd-Y14157 complex”. X-ray diffraction, 2 ligands (9QL, CO), 2 pockets (best druggability 0.68). MolNFT v1 #190432 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 7X5S
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: 9QL, CO
Pockets: 2 · best druggability 0.68

Structure

x-ray diffraction · 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	380	29% helix, 33% strand	P93836

Ligands and binding sites

9QL · 2-methyl-4-(2-nitro-4-piperidin-1-yl-phenyl)carbonyl-5-phenyl-1H-pyrazol-3-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	583	0.68	0.77	47	CO, 9QL
2	66	0.34	0.76	13	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

7X5S · Crystal structure of AtHPPD-Y14157 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 7X5S · PDBe 7X5S · UniProt P93836

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