Structure of PDB 1l8o Chain A

Receptor sequence
>1l8oA (length=222) Species: 9606 (Homo sapiens) [Search protein sequence]
HSELRKLFYSADAVCFDVDSTVIREEGIDELAKICGVEDAVSEMTRRAMG
GAVPFKAALTERLALIQPSREQVQRLIAEQPPHLTPGIRELVSRLQERNV
QVFLISGGFRSIVEHVASKLNIPATNVFANRLKFYFNGEYAGFDETQPTA
ESGGKGKVIKFLKEKFHFKKIIMIGDGATDMEACPPADAFIGFGGNVIRQ
QVKDNAKWYITDFVELLGELEE
3D structure
PDB1l8o Molecular basis for the local conformational rearrangement of human phosphoserine phosphatase
ChainA
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 PO4 A D20 D22 S109 K158 D17 D19 S106 K155
BS02 SER A G180 T182 R202 G177 T179 R199
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
PDBsum1l8o
PubMed12213811
UniProtP78330|SERB_HUMAN Phosphoserine phosphatase (Gene Name=PSPH)

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