Structure of PDB 2iei Chain A

Receptor sequence
>2ieiA (length=794) Species: 9986 (Oryctolagus cuniculus) [Search protein sequence]
QISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVATPRDYYFALAHTVRD
HLVGRWIRTQQHYYEKDPKRIYYLSLEFYMGRTLQNTMVNLALENACDEA
TYQLGLDMEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRY
EFGIFNQKICGGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGRVEHTSG
AKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAKAPYIQAVLDRNLAEN
ISRVLYPNDNFFEGKELRLKQEYFVVAATLQDIIRRFKSFDAFPDKVAIQ
LNDTHPSLAIPELMRVLVDLERLDWDKAWEVTVKTCAYTNHTVIPEALER
WPVHLLETLLPRHLQIIYEINQRFLNRVAAAFPGDVDRLRRMSLVEEGAV
KRINMAHLCIAGSHAVNGVARIHSEILKKTIFKDFYELEPHKFQNKTNGI
TPRRWLVLCNPGLAEIIAERIGEEYISDLDQLRKLLSYVDDEAFIRDVAK
VKQENKLKFAAYLEREYVHINPNSLFDVQVKRIHEYKRQLLNCLHVITLY
NRIKKEPNKFVVPRTVMIGGKAAPGYHMAKMIIKLITAIGDVVNHDPVVG
DRLRVIFLENYRVSLAEKVIPAADLSEQISTAGTEASGTGNMKFMLNGAL
TIGTMDGANVEMAEEAGEENFFIFGMRVEDVDRLDQRGYNAQEYYDRIPE
LRQIIEQLSSGFFSPKQPDLFKDIVNMLMHHDRFKVFADYEEYVKCQERV
SALYKNPREWTRMVIRNIATSGKFSSDRTIAQYAREIWGVEPSR
3D structure
PDB2iei Development of potent, orally active 1-substituted-3,4-dihydro-2-quinolone glycogen phosphorylase inhibitors.
ChainA
Resolution1.91 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) H341 K531 R532 K537 T639 K643
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 PLR A Y90 G134 G135 K568 Y648 R649 G675 T676 G677 K680 Y79 G123 G124 K531 Y611 R612 G638 T639 G640 K643
BS02 FRX A R60 W67 P188 E190 K191 A192 R49 W56 P177 E179 K180 A181 MOAD: ic50=0.121uM
BS03 FRX A T38 V40 F53 H57 T27 V29 F42 H46 MOAD: ic50=0.121uM
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:2iei, PDBe:2iei, PDBj:2iei
PDBsum2iei
PubMed17095214
UniProtP00489|PYGM_RABIT Glycogen phosphorylase, muscle form (Gene Name=PYGM)

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