Structure of PDB 1c8l Chain A Binding Site BS03

Receptor Information
>1c8l Chain A (length=812) Species: 9986 (Oryctolagus cuniculus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SDQEKRKQISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVATPRDYYFA
LAHTVRDHLVGRWIRTQQHYYEKDPKRIYYLSLEFYMGRTLQNTMVNLAL
ENACDEATYQLGLDMEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAA
YGYGIRYEFGIFNQKICGGWQMEEADDWLRYGNPWEKARPEFTLPVHFYG
RVEHTSQGAKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAKAPNGGYI
QAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDIIRRFKS
SNFDAFPDKVAIQLNDTHPSLAIPELMRVLVDLERLDWDKAWEVTVKTCA
YTNHTVLPEALERWPVHLLETLLPRHLQIIYEINQRFLNRVAAAFPGDVD
RLRRMSLVEEGAVKRINMAHLCIAGSHAVNGVARIHSEILKKTIFKDFYE
LEPHKFQNKTNGITPRRWLVLCNPGLAEIIAERIGEEYISDLDQLRKLLS
YVDDEAFIRDVAKVKQENKLKFAAYLEREYKVHINPNSLFDVQVKRIHEY
KRQLLNCLHVITLYNRIKKEPNKFVVPRTVMIGGKAAPGYHMAKMIIKLI
TAIGDVVNHDPVVGDRLRVIFLENYRVSLAEKVIPAADLSEQISTAGTEA
SGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENFFIFGMRVEDVDRLDQ
RGYNAQEYYDRIPELRQIIEQLSSGFFSPKQPDLFKDIVNMLMHHDRFKV
FADYEEYVKCQERVSALYKNPREWTRMVIRNIATSGKFSSDRTIAQYARE
IWGVEPSRQRLP
Ligand information
Ligand IDCFF
InChIInChI=1S/C8H10N4O2/c1-10-4-9-6-5(10)7(13)12(3)8(14)11(6)2/h4H,1-3H3
InChIKeyRYYVLZVUVIJVGH-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341Cn1cnc2N(C)C(=O)N(C)C(=O)c12
ACDLabs 10.04O=C2N(c1ncn(c1C(=O)N2C)C)C
OpenEye OEToolkits 1.5.0Cn1cnc2c1C(=O)N(C(=O)N2C)C
FormulaC8 H10 N4 O2
NameCAFFEINE;
3,7-DIHYDRO-1,3,7-TRIMETHYL-1H-PURINE-2,6-DIONE
ChEMBLCHEMBL113
DrugBankDB00201
ZINCZINC000000001084
PDB chain1c8l Chain A Residue 940 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1c8l Structural basis of the synergistic inhibition of glycogen phosphorylase a by caffeine and a potential antidiabetic drug.
Resolution2.3 Å
Binding residue
(original residue number in PDB)		F285 H571 A610 G612 Y613
Binding residue
(residue number reindexed from 1)		F272 H548 A587 G589 Y590
Annotation score1
Binding affinityMOAD: ic50=0.45mM
BindingDB: IC50=114000nM
Enzymatic activity
Catalytic site (original residue number in PDB) H377 K568 R569 K574 T676 K680
Catalytic site (residue number reindexed from 1) H354 K545 R546 K551 T653 K657
Enzyme Commision number 2.4.1.1: glycogen phosphorylase.
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004645 1,4-alpha-oligoglucan phosphorylase activity
GO:0008184 glycogen phosphorylase activity
GO:0016757 glycosyltransferase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0005977 glycogen metabolic process
GO:0005980 glycogen catabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0098723 skeletal muscle myofibril

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1c8l, PDBe:1c8l, PDBj:1c8l
PDBsum1c8l
PubMed11368311
UniProtP00489|PYGM_RABIT Glycogen phosphorylase, muscle form (Gene Name=PYGM)

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