Structure of PDB 1h5y Chain B Binding Site BS04
Receptor Information
>1h5y Chain B (length=253) Species:
13773
(Pyrobaculum aerophilum) [
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SHMALRIIPCLDIDGGAKVVVKGVNFQGIREVGDPVEMAVRYEEEGADEI
AILDITAAPEGRATFIDSVKRVAEAVSIPVLVGGGVRSLEDATTLFRAGA
DKVSVNTAAVRNPQLVALLAREFGSQSTVVAIDAKWNGEYYEVYVKGGRE
ATGLDAVKWAKEVEELGAGEILLTSIDRDGTGLGYDVELIRRVADSVRIP
VIASGGAGRVEHFYEAAAAGADAVLAASLFHFRVLSIAQVKRYLKERGVE
VRI
Ligand information
Ligand ID
GOL
InChI
InChI=1S/C3H8O3/c4-1-3(6)2-5/h3-6H,1-2H2
InChIKey
PEDCQBHIVMGVHV-UHFFFAOYSA-N
SMILES
Software
SMILES
OpenEye OEToolkits 1.7.0
C(C(CO)O)O
ACDLabs 12.01
CACTVS 3.370
OCC(O)CO
Formula
C3 H8 O3
Name
GLYCEROL;
GLYCERIN;
PROPANE-1,2,3-TRIOL
ChEMBL
CHEMBL692
DrugBank
DB09462
ZINC
ZINC000000895048
PDB chain
1h5y Chain B Residue 501 [
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Receptor-Ligand Complex Structure
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PDB
1h5y
Structure of Hisf, a Histidine Biosynthetic Protein from Pyrobaculum Aerophilum
Resolution
2.0 Å
Binding residue
(original residue number in PDB)
K22 G147 D179
Binding residue
(residue number reindexed from 1)
K22 G147 D179
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
D12 D133
Catalytic site (residue number reindexed from 1)
D12 D133
Enzyme Commision number
4.3.2.10
: imidazole glycerol-phosphate synthase.
Gene Ontology
Molecular Function
GO:0000107
imidazoleglycerol-phosphate synthase activity
GO:0016829
lyase activity
Biological Process
GO:0000105
L-histidine biosynthetic process
Cellular Component
GO:0005737
cytoplasm
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:1h5y
,
PDBe:1h5y
,
PDBj:1h5y
PDBsum
1h5y
PubMed
11679715
UniProt
Q8ZY16
|HIS6_PYRAE Imidazole glycerol phosphate synthase subunit HisF (Gene Name=hisF)
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