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Crystal structure of human hydroxyacid oxidase 1

Analyse Crystal structure of human hydroxyacid oxidase 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2NZL
Type: protein
Length: 339 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hydroxyacid oxidase 1
EC: 1.1.3.15
UniProt: Q9UJM8
Ligands: FMN, GLV
Pockets: 2 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hydroxyacid oxidase 1 (EC 1.1.3.15)	protein	339	47% helix, 14% strand	Q9UJM8

Ligands and binding sites

FMN · Flavin mononucleotide · ligand · chains A
GLV · Glyoxylic acid · ligand · 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	143	0.80	0.97	29	FMN, GLV
2	136	0.49	0.78	29	empty

Compared structures

2NZL · Crystal structure of human hydroxyacid oxidase 1 · the same entry in another collection · chain A against A, TM-score 1.00
Q9UJM8 · AlphaFold monomer V2.0 prediction for hydroxyacid oxidase 1 (Q9UJM8) · a predicted model of the same protein · 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 Q9UJM8
Elsewhere: RCSB PDB 2NZL · PDBe 2NZL · UniProt Q9UJM8

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