Structure of PDB 1pyg Chain B

Receptor sequence
>1pygB (length=791) Species: 9986 (Oryctolagus cuniculus) [Search protein sequence]
GVENVTELKKNFNRHLHFTLVKDRNVATPRDYYFALAHTVRDHLVGRWIR
TQQHYYEKDPKRIYYLSLEFYMGRTLQNTMVNLALENACDEATYQLGLDM
EELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQK
ICGGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGRVEHTSQGAKWVDTQ
VVLAMPYDTPVPGYRNNVVNTMRLWSAKAPQAVLDRNLAENISKELRLKQ
EYFVVAATLQDIIRRFKSSKFGCRDPVRTNFDAFPDKVAIQLNDTHPSLA
IPELMRVLVDLERLDWDKAWEVTVKTCAYTNHTVLPEALERWPVHLLETL
LPRHLQIIYEINQRFLNRVAAAFPGDVDRLRRMSLVEEGAVKRINMAHLC
IAGSHAVNGVARIHSEILKKTIFKDFYELEPHKFQNKTNGITPRRWLVLC
NPGLAEIIAERIGEEYISDLDQLRKLLSYVDDEAFIRDVAKVKQENKLKF
AAYLEREYKVHINPNSLFDVQVKRIHEYKRQLLNCLHVITLYNRIKKEPN
KFVVPRTVMIGGKAAPGYHMAKMIIKLITAIGDVVNHDPVVGDRLRVIFL
ENYRVSLAEKVIPAADLSEQISTAGTEASGTGNMKFMLNGALTIGTMDGA
NVEMAEEAGEENFFIFGMRVEDVDRLDQRGYNAQEYYDRIPELRQIIEQL
SSGFFSPKQPDLFKDIVNMLMHHDRFKVFADYEEYVKCQERVSALYKNPR
EWTRMVIRNIATSGKFSSDRTIAQYAREIWGVEPSRQRLPA
3D structure
PDB1pyg Structural basis for the activation of glycogen phosphorylase b by adenosine monophosphate.
ChainB
Resolution2.87 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) H332 K523 R524 K529 T631 K635
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 AMP B D42 N44 V45 D23 N25 V26 PDBbind-CN: -logKd/Ki=5.52,Kd=3uM
BS02 AMP B W67 Q71 Y75 R309 R310 F316 G317 W48 Q52 Y56 R264 R265 F271 G272 PDBbind-CN: -logKd/Ki=5.52,Kd=3uM
BS03 PDP B Y90 G135 K568 Y648 R649 G675 T676 G677 K680 Y71 G116 K523 Y603 R604 G630 T631 G632 K635
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:1pyg, PDBe:1pyg, PDBj:1pyg
PDBsum1pyg
PubMed1962195
UniProtP00489|PYGM_RABIT Glycogen phosphorylase, muscle form (Gene Name=PYGM)

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