Structure of PDB 3lg2 Chain C Binding Site BS02
Receptor Information
>3lg2 Chain C (length=269) Species:
559292
(Saccharomyces cerevisiae S288C) [
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SLTPRCIIVRHGQTEWSKSGQYTGLTDLPLTPYGEGQMLRTGESVFRNNQ
FLNPDNITYIFTSPRLRARQTVDLVLKPLSDEQRAKIRVVVDDDLREWEY
GDYEGMLTREIIELRKSRGLDKERPWNIWRDGCENGETTQQIGLRLSRAI
ARIQNLHRKHQSEGRASDIMVFAHGHALRYFAAIWFGLGVQKKCETIEEI
QNVKSYDDDTVPYVKLESYRHLVDNPCFLLDAGGIGVLSYAHHNIDEPAL
ELAGPFVSPPEEESQHGDV
Ligand information
Ligand ID
PO4
InChI
InChI=1S/H3O4P/c1-5(2,3)4/h(H3,1,2,3,4)/p-3
InChIKey
NBIIXXVUZAFLBC-UHFFFAOYSA-K
SMILES
Software
SMILES
CACTVS 3.341
[O-][P]([O-])([O-])=O
ACDLabs 10.04
[O-]P([O-])([O-])=O
OpenEye OEToolkits 1.5.0
[O-]P(=O)([O-])[O-]
Formula
O4 P
Name
PHOSPHATE ION
ChEMBL
DrugBank
DB14523
ZINC
PDB chain
3lg2 Chain C Residue 272 [
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Receptor-Ligand Complex Structure
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PDB
3lg2
Structure and activity of the metal-independent fructose-1,6-bisphosphatase YK23 from Saccharomyces cerevisiae.
Resolution
2.6 Å
Binding residue
(original residue number in PDB)
H244 H268
Binding residue
(residue number reindexed from 1)
H242 H266
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
H13 R69 E99
Catalytic site (residue number reindexed from 1)
H11 R67 E97
Enzyme Commision number
3.1.3.37
: sedoheptulose-bisphosphatase.
Gene Ontology
Molecular Function
GO:0016491
oxidoreductase activity
GO:0016787
hydrolase activity
GO:0050278
sedoheptulose-bisphosphatase activity
Biological Process
GO:0046390
ribose phosphate biosynthetic process
Cellular Component
GO:0005634
nucleus
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:3lg2
,
PDBe:3lg2
,
PDBj:3lg2
PDBsum
3lg2
PubMed
20427268
UniProt
P36136
|SHB17_YEAST Sedoheptulose 1,7-bisphosphatase (Gene Name=SHB17)
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