Structure of PDB 1e1y Chain A

Receptor sequence
>1e1yA (length=813) Species: 9986 (Oryctolagus cuniculus) [Search protein sequence]
SDQEKRKQISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVATPRDYYFA
LAHTVRDHLVGRWIRTQQHYYEKDPKRIYYLSLEFYMGRTLQNTMVNLAL
ENACDEATYQLGLDMEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAA
YGYGIRYEFGIFNQKICGGWQMEEADDWLRYGNPWEKARPEFTLPVHFYG
RVEHTSQGAKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAKAPNGYIQ
AVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDIIRRFKSN
FDAFPDKVAIQLNDTHPSLAIPELMRVLVDLERLDWDKAWEVTVKTCAYT
NHTVLPEALERWPVHLLETLLPRHLQIIYEINQRFLNRVAAAFPGDVDRL
RRMSLVEEGAVKRINMAHLCIAGSHAVNGVARIHSEILKKTIFKDFYELE
PHKFQNKTNGITPRRWLVLCNPGLAEIIAERIGEEYISDLDQLRKLLSYV
DDEAFIRDVAKVKQENKLKFAAYLEREYKVHINPNSLFDVQVKRIHEYKR
QLLNCLHVITLYNRIKKEPNKFVVPRTVMIGGKAAPGYHMAKMIIKLITA
IGDVVNHDPVVGDRLRVIFLENYRVSLAEKVIPAADLSEQISTAGTEASG
TGNMKFMLNGALTIGTMDGANVEMAEEAGEENFFIFGMRVEDVDRLDQRG
YNAQEYYDRIPELRQIIEQLSSGFFSPKQPDLFKDIVNMLMHHDRFKVFA
DYEEYVKCQERVSALYKNPREWTRMVIRNIATSGKFSSDRTIAQYAREIW
GVEPSRQRLPAPD
3D structure
PDB1e1y Flavopiridol Inhibits Glycogen Phosphorylase by Binding at the Inhibitor Site
ChainA
Resolution2.23 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H377 K568 R569 K574 T676 K680
Catalytic site (residue number reindexed from 1) H352 K543 R544 K549 T651 K655
Enzyme Commision number 2.4.1.1: glycogen phosphorylase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 CPB A N284 F285 L380 E382 A610 G612 Y613 N270 F271 L355 E357 A585 G587 Y588 MOAD: ic50=2.5uM
PDBbind-CN: -logKd/Ki=5.60,IC50=2.5uM
BindingDB: IC50=1200nM
BS02 PO3 A S14 V15 R69 S10 V11 R65
BS03 GLC A G135 L136 L139 N284 H377 N484 E672 G675 G131 L132 L135 N270 H352 N459 E647 G650
BS04 PLP A G134 K568 Y648 R649 V650 G675 T676 G677 K680 G130 K543 Y623 R624 V625 G650 T651 G652 K655
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:1e1y, PDBe:1e1y, PDBj:1e1y
PDBsum1e1y
PubMed10924512
UniProtP00489|PYGM_RABIT Glycogen phosphorylase, muscle form (Gene Name=PYGM)

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