Structure of PDB 4rkk Chain A Binding Site BS05

Receptor Information
>4rkk Chain A (length=317) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GSHMRFRFGVVVPPAVAGARPELLVVGSRPELGRWEPRGAVRLRPAGTAA
GDGALALQEPGLWLGEVELAARVDTFWYKFLKREPGGELSWEGNGPHHDR
CCTYNENNLVDGVYCLPIGHWIEATGHTNEMKHTTDFYFNIAGHQAMHYS
RILPNIWLGSCPRQVEHVTIKLKHELGITAVMNFQTEWDIVQNSSGCNRY
PEPMTPDTMIKLYREEGLAYIWMPTPDMSTEGRVQMLPQAVCLLHALLEK
GHIVYVHSNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRPAVYIDEE
ALARAQEDFFQKFGKVR
Ligand information
Ligand IDGLC
InChIInChI=1S/C6H12O6/c7-1-2-3(8)4(9)5(10)6(11)12-2/h2-11H,1H2/t2-,3-,4+,5-,6+/m1/s1
InChIKeyWQZGKKKJIJFFOK-DVKNGEFBSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C(C1C(C(C(C(O1)O)O)O)O)O
OpenEye OEToolkits 1.5.0C([C@@H]1[C@H]([C@@H]([C@H]([C@H](O1)O)O)O)O)O
CACTVS 3.341OC[CH]1O[CH](O)[CH](O)[CH](O)[CH]1O
CACTVS 3.341OC[C@H]1O[C@H](O)[C@H](O)[C@@H](O)[C@@H]1O
ACDLabs 10.04OC1C(O)C(OC(O)C1O)CO
FormulaC6 H12 O6
Namealpha-D-glucopyranose;
alpha-D-glucose;
D-glucose;
glucose
ChEMBLCHEMBL423707
DrugBank
ZINCZINC000003861213
PDB chain4rkk Chain E Residue 5 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB4rkk Structural mechanism of laforin function in glycogen dephosphorylation and lafora disease.
Resolution2.4 Å
Binding residue
(original residue number in PDB)		W32 P104 D107
Binding residue
(residue number reindexed from 1)		W35 P96 D99
Annotation score1
Enzymatic activity
Enzyme Commision number 3.1.3.-
3.1.3.16: protein-serine/threonine phosphatase.
3.1.3.48: protein-tyrosine-phosphatase.
Gene Ontology
Molecular Function
GO:0004373 alpha-1,4-glucan glucosyltransferase (UDP-glucose donor) activity
GO:0004721 phosphoprotein phosphatase activity
GO:0004722 protein serine/threonine phosphatase activity
GO:0004725 protein tyrosine phosphatase activity
GO:0005515 protein binding
GO:0016791 phosphatase activity
GO:0017018 myosin phosphatase activity
GO:0019203 carbohydrate phosphatase activity
GO:0030246 carbohydrate binding
GO:0030247 polysaccharide binding
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
GO:2001069 glycogen binding
GO:2001070 starch binding
Biological Process
GO:0000045 autophagosome assembly
GO:0001558 regulation of cell growth
GO:0005977 glycogen metabolic process
GO:0005978 glycogen biosynthetic process
GO:0006470 protein dephosphorylation
GO:0006816 calcium ion transport
GO:0006914 autophagy
GO:0007005 mitochondrion organization
GO:0007399 nervous system development
GO:0010468 regulation of gene expression
GO:0010629 negative regulation of gene expression
GO:0014009 glial cell proliferation
GO:0015813 L-glutamate transmembrane transport
GO:0016055 Wnt signaling pathway
GO:0016239 positive regulation of macroautophagy
GO:0016311 dephosphorylation
GO:0031396 regulation of protein ubiquitination
GO:0035335 peptidyl-tyrosine dephosphorylation
GO:0042306 regulation of protein import into nucleus
GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process
GO:0044042 glucan metabolic process
GO:0045786 negative regulation of cell cycle
GO:0046835 carbohydrate phosphorylation
GO:0046959 habituation
GO:0061136 regulation of proteasomal protein catabolic process
GO:1903076 regulation of protein localization to plasma membrane
Cellular Component
GO:0005634 nucleus
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0005783 endoplasmic reticulum
GO:0005789 endoplasmic reticulum membrane
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0030425 dendrite
GO:0043204 perikaryon
GO:0043231 intracellular membrane-bounded organelle
GO:0098554 cytoplasmic side of endoplasmic reticulum membrane
GO:0098556 cytoplasmic side of rough endoplasmic reticulum membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4rkk, PDBe:4rkk, PDBj:4rkk
PDBsum4rkk
PubMed25544560
UniProtO95278|EPM2A_HUMAN Laforin (Gene Name=EPM2A)

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