Structure of PDB 1zcl Chain B Binding Site BS01
Receptor Information
>1zcl Chain B (length=152) Species:
10116
(Rattus norvegicus) [
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PVEVTYKNMRFLITHNPTNATLNKFIEELKKYGVTTIVRVCEATYDTTLV
EKEGIHVLDWPFDDGAPPSNQIVDDWLSLVKIKFREEPGCCIAVHSVAGL
GRAPVLVALALIEGGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRL
RF
Ligand information
Ligand ID
SO4
InChI
InChI=1S/H2O4S/c1-5(2,3)4/h(H2,1,2,3,4)/p-2
InChIKey
QAOWNCQODCNURD-UHFFFAOYSA-L
SMILES
Software
SMILES
OpenEye OEToolkits 1.5.0
[O-]S(=O)(=O)[O-]
CACTVS 3.341
[O-][S]([O-])(=O)=O
ACDLabs 10.04
[O-]S([O-])(=O)=O
Formula
O4 S
Name
SULFATE ION
ChEMBL
DrugBank
DB14546
ZINC
PDB chain
1zcl Chain B Residue 4397 [
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Receptor-Ligand Complex Structure
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PDB
1zcl
Structure and Biochemical Properties of PRL-1, a Phosphatase Implicated in Cell Growth, Differentiation, and Tumor Invasion.
Resolution
2.9 Å
Binding residue
(original residue number in PDB)
S104 V105 A106 G109 R110
Binding residue
(residue number reindexed from 1)
S96 V97 A98 G101 R102
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
P25
Catalytic site (residue number reindexed from 1)
P17
Enzyme Commision number
3.1.3.48
: protein-tyrosine-phosphatase.
Gene Ontology
Molecular Function
GO:0004721
phosphoprotein phosphatase activity
GO:0004725
protein tyrosine phosphatase activity
Biological Process
GO:0006470
protein dephosphorylation
GO:0016311
dephosphorylation
GO:0030335
positive regulation of cell migration
Cellular Component
GO:0005634
nucleus
GO:0005737
cytoplasm
GO:0005768
endosome
GO:0005769
early endosome
GO:0005783
endoplasmic reticulum
GO:0005819
spindle
GO:0005856
cytoskeleton
GO:0005886
plasma membrane
GO:0009898
cytoplasmic side of plasma membrane
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:1zcl
,
PDBe:1zcl
,
PDBj:1zcl
PDBsum
1zcl
PubMed
16142898
UniProt
Q78EG7
|TP4A1_RAT Protein tyrosine phosphatase type IVA 1 (Gene Name=Ptp4a1)
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