Structure of PDB 1ci0 Chain A

Receptor sequence
>1ci0A (length=205) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
FTLNEKQLTDDPIDLFTKWFNEAKEDPRETLPEAITFSSAELPSGRVSSR
ILLFKELDHRGFTIYSNWGTSRKAHDIATNPNAAIVFFWKDLQRQVRVEG
ITEHVNRETSERYFKTRPRGSKIGAWASRQSDVIKNREELDELTQKNTER
FKDAEDIPCPDYWGGLRIVPLEIEFWQGRPSRLHDRFVYRRKTENDPWKV
VRLAP
3D structure
PDB1ci0 The Structure of PNP Oxidase from S. Cerevisiae
ChainA
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) R205
Catalytic site (residue number reindexed from 1) R182
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 FMN A R73 I74 L75 L76 Y88 S89 R95 K96 Q153 S154 R50 I51 L52 L53 Y65 S66 R72 K73 Q130 S131
BS02 FMN A F111 Q118 R120 W199 R209 F88 Q95 R97 W176 R186
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
Biological Process
GO:0008615 pyridoxine biosynthetic process
GO:0009443 pyridoxal 5'-phosphate salvage
GO:0042816 vitamin B6 metabolic process
GO:1901615 organic hydroxy compound metabolic process
Cellular Component
GO:0005739 mitochondrion
GO:0005758 mitochondrial intermembrane space

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:1ci0, PDBe:1ci0, PDBj:1ci0
PDBsum1ci0
PubMed
UniProtP38075|PDX3_YEAST Pyridoxamine 5'-phosphate oxidase (Gene Name=PDX3)

[Back to BioLiP]