Structure of PDB 1jnw Chain A

Receptor sequence

>1jnwA (length=214) Species: 562 (Escherichia coli)

DELQQIAHLRREYTKGGLRRRDLPADPLTLFERWLSQACEAKLADPTAMV
VATVDEHGQPYQRIVLLKHYDEKGMVFYTNLGSRKAHQIENNPRVSLLFP
WHTLERQVMVIGKAERLSTLEVMKYFHSRPRDSQIGAWVSKQSSRISARG
ILESKFLELKQKFQQGEVPLPSFWGGFRVSLEQIEFWQGGEHRLHDRFLY
QRENDAWKIDRLAP

3D structure

• PDB: 1jnw Active site structure and stereospecificity of Escherichia coli pyridoxine-5'-phosphate oxidase.
• Chain: A
• Resolution: 2.07 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R197
• Catalytic site (residue number reindexed from 1): R193
• Enzyme Commision number: 1.4.3.5: pyridoxal 5'-phosphate synthase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	PO4	A	R23 R24 F202 R215	R19 R20 F198 R211
BS02	FMN	A	Y17 Q111 W191 R201	Y13 Q107 W187 R197
BS03	PLP	A	R14 Y17 R197 H199	R10 Y13 R193 H195

Gene Ontology

Molecular Function

• GO:0004733 pyridoxamine phosphate oxidase activity
• GO:0010181 FMN binding
• GO:0016491 oxidoreductase activity
• GO:0016638 oxidoreductase activity, acting on the CH-NH2 group of donors
• GO:0030170 pyridoxal phosphate binding
• GO:0042301 phosphate ion binding
• GO:0042803 protein homodimerization activity
• GO:1902444 riboflavin binding

Biological Process

• GO:0008615 pyridoxine biosynthetic process
• GO:0036001 'de novo' pyridoxal 5'-phosphate biosynthetic process
• GO:0042816 vitamin B6 metabolic process
• GO:0042823 pyridoxal phosphate biosynthetic process
• GO:1901615 organic hydroxy compound metabolic process

Cellular Component

• GO:0005829 cytosol
• GO:0032991 protein-containing complex

External links

• PDB: RCSB:1jnw, PDBe:1jnw, PDBj:1jnw
• PDBsum: 1jnw
• PubMed: 11786019
• UniProt: P0AFI7|PDXH_ECOLI Pyridoxine/pyridoxamine 5'-phosphate oxidase (Gene Name=pdxH)