Structure of PDB 1g5b Chain C Binding Site BS03
Receptor Information
>1g5b Chain C (length=221) Species:
10710
(Lambdavirus lambda) [
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MRYYEKIDGSKYRNIWVVGDLHGCYTNLMNKLDTIGFDNKKDLLISVGDL
VDRGAENVECLELITFPWFRAVRGNHEQMMIDGLSERGNVNHWLLNGGGW
FFNLDYDKEILAKALAHKADELPLIIELVSKDKKYVICHADYPFDEYEFG
KPVDHQQVIWNRERISNSQNGIVKEIKGADTFIFGHTPAVKPLKFANQMY
IDTGAVFCGNLTLIQVQGAGA
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
1g5b Chain C Residue 3003 [
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Receptor-Ligand Complex Structure
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PDB
1g5b
Structure of the bacteriophage lambda Ser/Thr protein phosphatase with sulfate ion bound in two coordination modes.
Resolution
2.15 Å
Binding residue
(original residue number in PDB)
H22 D49 R53 N75 H76 H186
Binding residue
(residue number reindexed from 1)
H22 D49 R53 N75 H76 H186
Annotation score
1
Enzymatic activity
Enzyme Commision number
3.1.3.16
: protein-serine/threonine phosphatase.
Gene Ontology
Molecular Function
GO:0004721
phosphoprotein phosphatase activity
GO:0004722
protein serine/threonine phosphatase activity
GO:0005515
protein binding
GO:0008803
bis(5'-nucleosyl)-tetraphosphatase (symmetrical) activity
GO:0016787
hydrolase activity
GO:0016791
phosphatase activity
GO:0017018
myosin phosphatase activity
GO:0046872
metal ion binding
Biological Process
GO:0110154
RNA decapping
Cellular Component
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:1g5b
,
PDBe:1g5b
,
PDBj:1g5b
PDBsum
1g5b
PubMed
11112522
UniProt
P03772
|PP_LAMBD Serine/threonine-protein phosphatase
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