Structure of PDB 1ww2 Chain A

Receptor sequence
>1ww2A (length=817) Species: 9986 (Oryctolagus cuniculus) [Search protein sequence]
QISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVATPRDYYFALAHTVRD
HLVGRWIRTQQHYYEKDPKRIYYLSLEFYMGRTLQNTMVNLALENACDEA
TYQLGLDMEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRY
EFGIFNQKICGGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGRVEHTSQ
GAKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAKAPNDFNLKDFNVGG
YIQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDIIRRF
KSSTNFDAFPDKVAIQLNDTHPSLAIPELMRVLVDLERLDWDKAWEVTVK
TCAYTNHTVIPEALERWPVHLLETLLPRHLQIIYEINQRFLNRVAAAFPG
DVDRLRRMSLVEEGAVKRINMAHLCIAGSHAVNGVARIHSEILKKTIFKD
FYELEPHKFQNKTNGITPRRWLVLCNPGLAEIIAERIGEEYISDLDQLRK
LLSYVDDEAFIRDVAKVKQENKLKFAAYLEREYKVHINPNSLFDVQVKRI
HEYKRQLLNCLHVITLYNRIKKEPNKFVVPRTVMIGGKAAPGYHMAKMII
KLITAIGDVVNHDPVVGDRLRVIFLENYRVSLAEKVIPAADLSEQISTAG
TEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENFFIFGMRVEDVDR
LDQRGYNAQEYYDRIPELRQIIEQLSSGFFSPKQPDLFKDIVNMLMHHDR
FKVFADYEEYVKCQERVSALYKNPREWTRMVIRNIATSGKFSSDRTIAQY
AREIWGVEPSRQRLPAP
3D structure
PDB1ww2 Crystallographic studies on two bioisosteric analogues, N-acetyl-beta-d-glucopyranosylamine and N-trifluoroacetyl-beta-d-glucopyranosylamine, potent inhibitors of muscle glycogen phosphorylase
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) H357 K548 R549 K554 T656 K660
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 NBG A N284 H377 N484 E672 G675 N273 H357 N464 E652 G655 MOAD: Ki=32uM
BindingDB: Ki=32000nM
BS02 PLP A G134 G135 K568 Y648 R649 V650 G675 T676 G677 K680 G123 G124 K548 Y628 R629 V630 G655 T656 G657 K660
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:1ww2, PDBe:1ww2, PDBj:1ww2
PDBsum1ww2
PubMed16213146
UniProtP00489|PYGM_RABIT Glycogen phosphorylase, muscle form (Gene Name=PYGM)

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