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Active site structure of E. COLI pyridoxine 5'-phosphate oxidase

Analyse Active site structure of E. COLI pyridoxine 5'-phosphate oxidase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1JNW
Type: protein
Length: 214 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pyridoxine 5'-phosphate oxidase
EC: 1.4.3.5
UniProt: P28225
Ligands: FMN, PLP, PO4
Pockets: 1 · best druggability 0.34

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Pyridoxine 5'-phosphate oxidase (EC 1.4.3.5)	protein	214	31% helix, 32% strand	P28225

Ligands and binding sites

FMN · Flavin mononucleotide · ligand · chains A
PLP · Pyridoxal-5'-phosphate · ligand · chains A
PO4 · Phosphate ion · ion · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	97	0.34	0.74	18	empty

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

1JNW · Active Site Structure of E. coli pyridoxine 5'-phosphate Oxidase · 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 P28225
Elsewhere: RCSB PDB 1JNW · PDBe 1JNW · UniProt P28225

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