Structure of PDB 6hyj Chain B Binding Site BS03
Receptor Information
>6hyj Chain B (length=223) Species:
9606
(Homo sapiens) [
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MISHSELRKLFYSADAVCFDVDSTVIREEGIDELAKICGVEDAVSEMTRR
AMGGAVPFKAALTERLALIQPSREQVQRLIAEQPPHLTPGIRELVSRLQE
RNVQVFLISGGFRSIVEHVASKLNIPATNVFANRLKFYFNGEYAGFDETQ
PTAESGGKGKVIKLLKEKFHFKKIIMIGDGATDMEACPPADAFIGFGGNV
IRQQVKDNAKWYITDFVELLGEL
Ligand information
Ligand ID
SER
InChI
InChI=1S/C3H7NO3/c4-2(1-5)3(6)7/h2,5H,1,4H2,(H,6,7)/t2-/m0/s1
InChIKey
MTCFGRXMJLQNBG-REOHCLBHSA-N
SMILES
Software
SMILES
CACTVS 3.341
N[CH](CO)C(O)=O
OpenEye OEToolkits 1.5.0
C(C(C(=O)O)N)O
CACTVS 3.341
N[C@@H](CO)C(O)=O
ACDLabs 10.04
O=C(O)C(N)CO
OpenEye OEToolkits 1.5.0
C([C@@H](C(=O)O)N)O
Formula
C3 H7 N O3
Name
SERINE
ChEMBL
CHEMBL11298
DrugBank
DB00133
ZINC
ZINC000000895034
PDB chain
6hyj Chain B Residue 303 [
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Receptor-Ligand Complex Structure
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PDB
6hyj
Crystal structures and snapshots along the reaction pathway of human phosphoserine phosphatase.
Resolution
1.929 Å
Binding residue
(original residue number in PDB)
E29 R202
Binding residue
(residue number reindexed from 1)
E29 R202
Annotation score
5
Enzymatic activity
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:6hyj
,
PDBe:6hyj
,
PDBj:6hyj
PDBsum
6hyj
PubMed
31205021
UniProt
P78330
|SERB_HUMAN Phosphoserine phosphatase (Gene Name=PSPH)
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