Structure of PDB 1g78 Chain A

Receptor sequence

>1g78A (length=199) Species: 562 (Escherichia coli)

GGLRRRDLPADPLTLFERWLSQACEAKLADPTAMVVATVDEHGQPYQRIV
LLKHYDEKGMVFYTNLGSRKAHQIENNPRVSLLFPWHTLERQVMVIGKAE
RLSTLEVMKYFHSRPRDSQIGAWVSKQSSRISARGILESKFLELKQKFQQ
GEVPLPSFWGGFRVSLEQIEFWQGGEHRLHDRFLYQRENDAWKIDRLAP

3D structure

• PDB: 1g78 X-ray structure of Escherichia coli pyridoxine 5'-phosphate oxidase complexed with pyridoxal 5'-phosphate at 2.0 A resolution.
• Chain: A
• Resolution: 2.2 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R197
• Catalytic site (residue number reindexed from 1): R178
• 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 R215	R4 R5 R196
BS02	FMN	A	R67 I68 V69 L70 Y82 T83 R88 K89 Q146 S147	R48 I49 V50 L51 Y63 T64 R69 K70 Q127 S128
BS03	PLP	A	Y129 R133	Y110 R114
BS04	PLP	A	S144 K145 F177	S125 K126 F158

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:1g78, PDBe:1g78, PDBj:1g78
• PDBsum: 1g78
• PubMed: 11453690
• UniProt: P0AFI7|PDXH_ECOLI Pyridoxine/pyridoxamine 5'-phosphate oxidase (Gene Name=pdxH)