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BioLiP

Structure of PDB 1znn Chain C Binding Site BS01

Receptor Information
>1znn Chain C (length=245) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KGGVIMDVVNAEQAKIAEAAGAVAVMALEGGVARMADPTVIEEVMNAVSI
PVMAKVRIGHYVEARVLEALGVDYIDESEVLTPADEEFHIDKRQFTVPFV
CGCRDLGEAARRIAEGASMLRTKGEPGTGNIVEAVRHMRKVNAQIRKVVN
MSEDELVAEAKQLGAPVEVLREIKRLGRLPVVNFAAGGVTTPADAALMMH
LGADGVFVGSGIFKSENPEKYARAIVEATTHYEDYELIAHLSKGL
Ligand information
Ligand IDSO4
InChIInChI=1S/H2O4S/c1-5(2,3)4/h(H2,1,2,3,4)/p-2
InChIKeyQAOWNCQODCNURD-UHFFFAOYSA-L
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0[O-]S(=O)(=O)[O-]
CACTVS 3.341[O-][S]([O-])(=O)=O
ACDLabs 10.04[O-]S([O-])(=O)=O
FormulaO4 S
NameSULFATE ION
ChEMBL
DrugBankDB14546
ZINC
PDB chain1znn Chain C Residue 2406 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1znn A New Arrangement of (beta/alpha)8 Barrels in the Synthase Subunit of PLP Synthase.
Resolution2.2 Å
Binding residue
(original residue number in PDB)		G153 G155 G214
Binding residue
(residue number reindexed from 1)		G127 G129 G188
Annotation score1
Enzymatic activity
Enzyme Commision number 4.3.3.6: pyridoxal 5'-phosphate synthase (glutamine hydrolyzing).
Gene Ontology
Molecular Function
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:0008615 pyridoxine biosynthetic process
GO:0042819 vitamin B6 biosynthetic process
GO:0042823 pyridoxal phosphate biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1znn, PDBe:1znn, PDBj:1znn
PDBsum1znn
PubMed15911615
UniProtQ5L3Y2|PDXS_GEOKA Pyridoxal 5'-phosphate synthase subunit PdxS (Gene Name=pdxS)

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