Structure of PDB 2ieg Chain A

Receptor sequence
>2iegA (length=803) Species: 9986 (Oryctolagus cuniculus) [Search protein sequence]
QISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVATPRDYYFALAHTVRD
HLVGRWIRTQQHYYEKDPKRIYYLSLEFYMGRTLQNTMVNLALENACDEA
TYQLGLDMEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRY
EFGIFNQKICGGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGRVEHTQG
AKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAKAPNGGYIQAVLDRNL
AENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDIIRRFKSNFDAFPDK
VAIQLNDTHPSLAIPELMRVLVDLERLDWDKAWEVTVKTCAYTNHTVIPE
ALERWPVHLLETLLPRHLQIIYEINQRFLNRVAAAFPGDVDRLRRMSLVE
EGAVKRINMAHLCIAGSHAVNGVARIHSEILKKTIFKDFYELEPHKFQNK
TNGITPRRWLVLCNPGLAEIIAERIGEEYISDLDQLRKLLSYVDDEAFIR
DVAKVKQENKLKFAAYLEREYKVHINPNSLFDVQVKRIHEYKRQLLNCLH
VITLYNRIKKEPNKFVVPRTVMIGGKAAPGYHMAKMIIKLITAIGDVVNH
DPVVGDRLRVIFLENYRVSLAEKVIPAADLSEQISTAGTEASGTGNMKFM
LNGALTIGTMDGANVEMAEEAGEENFFIFGMRVEDVDRLDQRGYNAQEYY
DRIPELRQIIEQLSSGFFSPKQPDLFKDIVNMLMHHDRFKVFADYEEYVK
CQERVSALYKNPREWTRMVIRNIATSGKFSSDRTIAQYAREIWGVEPSRQ
RLP
3D structure
PDB2ieg Development of potent, orally active 1-substituted-3,4-dihydro-2-quinolone glycogen phosphorylase inhibitors.
ChainA
Resolution1.9 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) H345 K536 R537 K542 T644 K648
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 G134 K568 Y648 R649 V650 G675 T676 G677 K680 G123 K536 Y616 R617 V618 G643 T644 G645 K648
BS02 FRY A R60 W67 P188 E190 K191 A192 R49 W56 P177 E179 K180 A181 MOAD: ic50=0.135uM
BS03 FRY A T38 V40 F53 H57 Y185 T27 V29 F42 H46 Y174 MOAD: ic50=0.135uM
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:2ieg, PDBe:2ieg, PDBj:2ieg
PDBsum2ieg
PubMed17095214
UniProtP00489|PYGM_RABIT Glycogen phosphorylase, muscle form (Gene Name=PYGM)

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