Structure of PDB 5a68 Chain A Binding Site BS02
Receptor Information
>5a68 Chain A (length=203) Species:
3702
(Arabidopsis thaliana) [
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GAMEVEVKLRLLTAAAHLRLTTLLTPYHLKTLHQRNTFFDTPKNDLSLRR
AVLRLRFLQNAPSPPRCIVSLKAKPTLANGISRVEEDEEEIEYWIGKECV
ESPAKLSDIGSRVLKRVKEEYGFNDFLGFVCLGGFENVRNVYEWRGVKLE
VDETKYDFGNCYEIECETEEPERVKTMIEEFLTEEKIEFSNSDMTKFAVF
RSG
Ligand information
Ligand ID
MN
InChI
InChI=1S/Mn/q+2
InChIKey
WAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mn+2]
CACTVS 3.341
[Mn++]
Formula
Mn
Name
MANGANESE (II) ION
ChEMBL
DrugBank
DB06757
ZINC
PDB chain
5a68 Chain A Residue 501 [
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Receptor-Ligand Complex Structure
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PDB
5a68
Structural Determinants for Substrate Binding and Catalysis in Triphosphate Tunnel Metalloenzymes.
Resolution
1.67 Å
Binding residue
(original residue number in PDB)
E4 E169
Binding residue
(residue number reindexed from 1)
E6 E165
Annotation score
1
Enzymatic activity
Enzyme Commision number
3.6.1.-
3.6.1.25
: triphosphatase.
Gene Ontology
Molecular Function
GO:0005524
ATP binding
GO:0016462
pyrophosphatase activity
GO:0016787
hydrolase activity
GO:0016887
ATP hydrolysis activity
GO:0050355
inorganic triphosphate phosphatase activity
Biological Process
GO:0048364
root development
Cellular Component
GO:0005634
nucleus
GO:0005680
anaphase-promoting complex
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:5a68
,
PDBe:5a68
,
PDBj:5a68
PDBsum
5a68
PubMed
26221030
UniProt
Q9SIY3
|TTM3_ARATH Triphosphate tunnel metalloenzyme 3 (Gene Name=TTM3)
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