Structure of PDB 2qn8 Chain A

Receptor sequence
>2qn8A (length=809) Species: 9986 (Oryctolagus cuniculus) [Search protein sequence]
QISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVATPRDYYFALAHTVRD
HLVGRWIRTQQHYYEKDPKRIYYLSLEFYMGRTLQNTMVNLALENACDEA
TYQLGLDMEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRY
EFGIFNQKICGGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGRVEHTSQ
GAKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAKAPNDVGGYIQAVLD
RNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDIIRRFKSSTNFD
AFPDKVAIQLNDTHPSLAIPELMRVLVDLERLDWDKAWEVTVKTCAYTNH
TVIPEALERWPVHLLETLLPRHLQIIYEINQRFLNRVAAAFPGDVDRLRR
MSLVEEGAVKRINMAHLCIAGSHAVNGVARIHSEILKKTIFKDFYELEPH
KFQNKTNGITPRRWLVLCNPGLAEIIAERIGEEYISDLDQLRKLLSYVDD
EAFIRDVAKVKQENKLKFAAYLEREYKVHINPNSLFDVQVKRIHEYKRQL
LNCLHVITLYNRIKKEPNKFVVPRTVMIGGKAAPGYHMAKMIIKLITAIG
DVVNHDPVVGDRLRVIFLENYRVSLAEKVIPAADLSEQISTAGTEASGTG
NMKFMLNGALTIGTMDGANVEMAEEAGEENFFIFGMRVEDVDRLDQRGYN
AQEYYDRIPELRQIIEQLSSGFFSPKQPDLFKDIVNMLMHHDRFKVFADY
EEYVKCQERVSALYKNPREWTRMVIRNIATSGKFSSDRTIAQYAREIWGV
EPSRQRLPA
3D structure
PDB2qn8 N-(4-substituted-benzoyl)-N'-(beta-D-glucopyranosyl)ureas, inhibitors of glycogen phosphorylase: synthesis, kinetic and crystallographic evaluation
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) H350 K541 R542 K547 T649 K653
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 PLP A Y90 G134 K568 Y648 R649 V650 G675 T676 G677 K680 Y79 G123 K541 Y621 R622 V623 G648 T649 G650 K653
BS02 NBY A R60 V64 W67 W189 E190 K191 P229 R49 V53 W56 W178 E179 K180 P218 BindingDB: Ki=3300nM
BS03 NBY A G135 L136 N282 D283 F286 H341 H377 N484 E672 A673 S674 G675 G124 L125 N264 D265 F268 H314 H350 N457 E645 A646 S647 G648 BindingDB: Ki=3300nM
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:2qn8, PDBe:2qn8, PDBj:2qn8
PDBsum2qn8
PubMed
UniProtP00489|PYGM_RABIT Glycogen phosphorylase, muscle form (Gene Name=PYGM)

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