Structure of PDB 1xl1 Chain A Binding Site BS01

Receptor Information
>1xl1 Chain A (length=810) Species: 9986 (Oryctolagus cuniculus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
QISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVATPRDYYFALAHTVRD
HLVGRWIRTQQHYYEKDPKRIYYLSLEFYMGRTLQNTMVNLALENACDEA
TYQLGLDMEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRY
EFGIFNQKICGGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGRVEHTSQ
GAKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAKAPNDFNLGYIQAVL
DRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDIIRRFKSSTNF
DAFPDKVAIQLNDTHPSLAIPELMRVLVDLERLDWDKAWEVTVKTCAYTN
HTVLPEALERWPVHLLETLLPRHLQIIYEINQRFLNRVAAAFPGDVDRLR
RMSLVEEGAVKRINMAHLCIAGSHAVNGVARIHSEILKKTIFKDFYELEP
HKFQNKTNGITPRRWLVLCNPGLAEIIAERIGEEYISDLDQLRKLLSYVD
DEAFIRDVAKVKQENKLKFAAYLEREYKVHINPNSLFDVQVKRIHEYKRQ
LLNCLHVITLYNRIKKEPNKFVVPRTVMIGGKAAPGYHMAKMIIKLITAI
GDVVNHDPVVGDRLRVIFLENYRVSLAEKVIPAADLSEQISTAGTEASGT
GNMKFMLNGALTIGTMDGANVEMAEEAGEENFFIFGMRVEDVDRLDQRGY
NAQEYYDRIPELRQIIEQLSSGFFSPKQPDLFKDIVNMLMHHDRFKVFAD
YEEYVKCQERVSALYKNPREWTRMVIRNIATSGKFSSDRTIAQYAREIWG
VEPSRQRLPA
Ligand information
Ligand IDTH1
InChIInChI=1S/C14H17NO5S/c1-6-2-3-9-7(4-6)15-14(21-9)13-12(19)11(18)10(17)8(5-16)20-13/h2-4,8,10-13,16-19H,5H2,1H3/t8-,10-,11+,12-,13-/m1/s1
InChIKeyWGJFWQVWYRZPEP-KABOQKQYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6Cc1ccc2c(c1)nc(s2)C3C(C(C(C(O3)CO)O)O)O
OpenEye OEToolkits 1.7.6Cc1ccc2c(c1)nc(s2)[C@H]3[C@@H]([C@H]([C@@H]([C@H](O3)CO)O)O)O
CACTVS 3.370Cc1ccc2sc(nc2c1)[C@@H]3O[C@H](CO)[C@@H](O)[C@H](O)[C@H]3O
CACTVS 3.370Cc1ccc2sc(nc2c1)[CH]3O[CH](CO)[CH](O)[CH](O)[CH]3O
ACDLabs 12.01n1c3cc(ccc3sc1C2OC(CO)C(O)C(O)C2O)C
FormulaC14 H17 N O5 S
Name(1R)-1,5-anhydro-1-(5-methyl-1,3-benzothiazol-2-yl)-D-glucitol;
2-(BETA-D-GLUCOPYRANOSYL)-5-METHYL-BENZOTHIAZOLE;
2-(BETA-D-GLUCOPYRANOSYL)-5-METHYL-1,3,4-BENZOTHIAZOLE
ChEMBL
DrugBankDB03250
ZINCZINC000038378861
PDB chain1xl1 Chain A Residue 998 [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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PDB1xl1 Kinetic and crystallographic studies on 2-(beta-D-glucopyranosyl)-5-methyl-1, 3, 4-oxadiazole, -benzothiazole, and -benzimidazole, inhibitors of muscle glycogen phosphorylase b. Evidence for a new binding site
Resolution2.1 Å
Binding residue
(original residue number in PDB)		L136 N284 H341 H377 T378 N484 E672 S674 G675
Binding residue
(residue number reindexed from 1)		L125 N267 H315 H351 T352 N458 E646 S648 G649
Annotation score1
Binding affinityMOAD: Ki=76uM
BindingDB: Ki=76000nM
Enzymatic activity
Catalytic site (original residue number in PDB) H377 K568 R569 K574 T676 K680
Catalytic site (residue number reindexed from 1) H351 K542 R543 K548 T650 K654
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1xl1, PDBe:1xl1, PDBj:1xl1
PDBsum1xl1
PubMed15741340
UniProtP00489|PYGM_RABIT Glycogen phosphorylase, muscle form (Gene Name=PYGM)

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