MolNFT v1 · #142293 · protein

The crystal structure of mandelate oxidase mutant Y128F with L-lactate

5ZZY · 4-hydroxymandelate oxidase: “The crystal structure of mandelate oxidase mutant Y128F with L-lactate”. X-ray diffraction, 2 ligands (FMN, 2OP), 3 pockets (best druggability 0.77). MolNFT v1 #142293 on GenesisL1: 3D structure, binding…

PDB: 5ZZY
Type: protein
Length: 333 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 4-hydroxymandelate oxidase
EC: 1.1.3.46
UniProt: O52792
Ligands: FMN, 2OP
Pockets: 3 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	4-hydroxymandelate oxidase (EC 1.1.3.46)	protein	333	44% helix, 15% strand	O52792

Ligands and binding sites

FMN · Flavin mononucleotide · ligand · chains A
2OP · (2S)-2-hydroxypropanoic acid · ligand · 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	270	0.77	0.89	43	FMN, 2OP
2	108	0.37	0.74	24	empty
3	81	0.35	0.75	15	empty

Compared structures

5ZZY · The crystal structure of Mandelate oxidase mutant Y128F with L-Lactate · the same entry in another collection · chain A against A, TM-score 1.00
O52792 · AlphaFold monomer V2.0 prediction for 4-hydroxymandelate oxidase (O52792) · 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 O52792
Elsewhere: RCSB PDB 5ZZY · PDBe 5ZZY · UniProt O52792

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