Structure of PDB 1l8o Chain A Binding Site BS01
Receptor Information
>1l8o Chain A (length=222) Species:
9606
(Homo sapiens) [
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HSELRKLFYSADAVCFDVDSTVIREEGIDELAKICGVEDAVSEMTRRAMG
GAVPFKAALTERLALIQPSREQVQRLIAEQPPHLTPGIRELVSRLQERNV
QVFLISGGFRSIVEHVASKLNIPATNVFANRLKFYFNGEYAGFDETQPTA
ESGGKGKVIKFLKEKFHFKKIIMIGDGATDMEACPPADAFIGFGGNVIRQ
QVKDNAKWYITDFVELLGELEE
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
1l8o Chain A Residue 901 [
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Receptor-Ligand Complex Structure
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PDB
1l8o
Molecular basis for the local conformational rearrangement of human phosphoserine phosphatase
Resolution
2.8 Å
Binding residue
(original residue number in PDB)
D20 D22 S109 K158
Binding residue
(residue number reindexed from 1)
D17 D19 S106 K155
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
D20 V21 D22 G110 K158 D183
Catalytic site (residue number reindexed from 1)
D17 V18 D19 G107 K155 D180
Enzyme Commision number
3.1.3.3
: phosphoserine phosphatase.
Gene Ontology
Molecular Function
GO:0000287
magnesium ion binding
GO:0016787
hydrolase activity
GO:0036424
L-phosphoserine phosphatase activity
GO:0042802
identical protein binding
GO:0042803
protein homodimerization activity
GO:0046872
metal ion binding
Biological Process
GO:0001701
in utero embryonic development
GO:0006563
L-serine metabolic process
GO:0006564
L-serine biosynthetic process
GO:0009612
response to mechanical stimulus
GO:0031667
response to nutrient levels
GO:0033574
response to testosterone
Cellular Component
GO:0005737
cytoplasm
GO:0005829
cytosol
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:1l8o
,
PDBe:1l8o
,
PDBj:1l8o
PDBsum
1l8o
PubMed
12213811
UniProt
P78330
|SERB_HUMAN Phosphoserine phosphatase (Gene Name=PSPH)
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