Structure of PDB 3o05 Chain B

Receptor sequence
>3o05B (length=261) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
MLKGGVIMDVVTPEQAKIAEKSGACAVMALESIPADMRKSGKVCRMSDPK
MIKDIMNSVSIPVMAKVRIGHFVEAQIIEALEVDYIDESEVLTPADWTHH
IEKDKFKVPFVCGAKDLGEALRRINEGAAMIRTKGEAGTGDVSEAVKHIR
RITEEIKACQQLKSEDDIAKVAEEMRVPVSLLKDVLEKGKLPVVNFAAGG
VATPADAALLMQLGCDGVFVGSGIFKSSNPVRLATAVVEATTHFDNPSKL
LEVSSDLGELM
3D structure
PDB3o05 Structural insights into the catalytic mechanism of the yeast pyridoxal 5-phosphate synthase Snz1
ChainB
Resolution2.2 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 4.3.3.6: pyridoxal 5'-phosphate synthase (glutamine hydrolyzing).
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 PLP B I83 W111 H114 R136 R137 K148 I69 W97 H100 R122 R123 K134
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0016829 lyase activity
GO:0016843 amine-lyase activity
GO:0036381 pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity
Biological Process
GO:0006520 amino acid metabolic process
GO:0006543 glutamine catabolic process
GO:0008615 pyridoxine biosynthetic process
GO:0042819 vitamin B6 biosynthetic process
GO:0042823 pyridoxal phosphate biosynthetic process
GO:1901617 organic hydroxy compound biosynthetic process
Cellular Component
GO:1903600 glutaminase complex

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Molecular Function
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Cellular Component
External links
PDB RCSB:3o05, PDBe:3o05, PDBj:3o05
PDBsum3o05
PubMed20919991
UniProtQ03148|SNZ1_YEAST Pyridoxal 5'-phosphate synthase subunit SNZ1 (Gene Name=SNZ1)

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