Structure of PDB 2qrp Chain A

Receptor sequence
>2qrpA (length=811) Species: 9986 (Oryctolagus cuniculus) [Search protein sequence]
RKQISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVATPRDYYFALAHTV
RDHLVGRWIRTQQHYYEKDPKRIYYLSLEFYMGRTLQNTMVNLALENACD
EATYQLGLDMEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGI
RYEFGIFNQKICGGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGRVEHT
SQGAKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAKAPNDNVGGYIQA
VLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDIIRRFKSSK
NFDAFPDKVAIQLNDTHPSLAIPELMRVLVDLERLDWDKAWEVTVKTCAY
TNHTVLPEALERWPVHLLETLLPRHLQIIYEINQRFLNRVAAAFPGDVDR
LRRMSLVEEGAVKRINMAHLCIAGSHAVNGVARIHSEILKKTIFKDFYEL
EPHKFQNKTNGITPRRWLVLCNPGLAEIIAERIGEEYISDLDQLRKLLSY
VDDEAFIRDVAKVKQENKLKFAAYLEREYKVHINPNSLFDVQVKRIHEYK
RQLLNCLHVITLYNRIKKEPNKFVVPRTVMIGGKAAPGYHMAKMIIKLIT
AIGDVVNHDPVVGDRLRVIFLENYRVSLAEKVIPAADLSEQISTAGTEAS
GTGNMKFMLNGALTIGTMDGANVEMAEEAGEENFFIFGMRVEDVDRLDQR
GYNAQEYYDRIPELRQIIEQLSSGFFSPKQPDLFKDIVNMLMHHDRFKVF
ADYEEYVKCQERVSALYKNPREWTRMVIRNIATSGKFSSDRTIAQYAREI
WGVEPSRQRLP
3D structure
PDB2qrp Glucose-based spiro-isoxazolines: a new family of potent glycogen phosphorylase inhibitors.
ChainA
Resolution1.86 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) H377 K568 R569 K574 T676 K680
Catalytic site (residue number reindexed from 1) H353 K544 R545 K550 T652 K656
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 S06 A L136 N282 N284 F285 H341 H377 A383 V455 N484 E672 S674 G675 L127 N267 N269 F270 H317 H353 A359 V431 N460 E648 S650 G651 MOAD: Ki=0.63uM
PDBbind-CN: -logKd/Ki=6.20,Ki=0.63uM
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2qrp, PDBe:2qrp, PDBj:2qrp
PDBsum2qrp
PubMed19781947
UniProtP00489|PYGM_RABIT Glycogen phosphorylase, muscle form (Gene Name=PYGM)

[Back to BioLiP]