Structure of PDB 1wv4 Chain A

Receptor sequence

>1wv4A (length=162) Species: 562 (Escherichia coli)

AHLRREYTKGGLRRRDLPADPLTLFERWLSQACEAKLADPTAMVVATVDE
HGQPYQRIVLLKHYDEKGMVFYTNLGSRKAHQIENNPRVSLLFPWHTLER
QVMVIGKAERLSTLEVMKYSFWGGFRVSLEQIEFWQGGEHRLHDRFLYQR
ENDAWKIDRLAP

3D structure

• PDB: 1wv4 Structure of Escherichia coli pyridoxine 5'-phosphate oxidase in a tetragonal crystal form: insights into the mechanistic pathway of the enzyme.
• Chain: A
• Resolution: 2.6 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R197
• Catalytic site (residue number reindexed from 1): R141
• 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	R24 R215	R14 R159
BS02	FMN	A	D49 R67 I68 V69 L70 Y82 T83 S87 R88 K89	D39 R57 I58 V59 L60 Y72 T73 S77 R78 K79
BS03	FMN	A	Q111 W191 R201	Q101 W135 R145

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:1wv4, PDBe:1wv4, PDBj:1wv4
• PDBsum: 1wv4
• PubMed: 15858270
• UniProt: P0AFI7|PDXH_ECOLI Pyridoxine/pyridoxamine 5'-phosphate oxidase (Gene Name=pdxH)