Structure of PDB 8gpb Chain A

Receptor sequence
>8gpbA (length=832) Species: 9986 (Oryctolagus cuniculus) [Search protein sequence]
KQISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVATPRDYYFALAHTVR
DHLVGRWIRTQQHYYEKDPKRIYYLSLEFYMGRTLQNTMVNLALENACDE
ATYQLGLDMEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIR
YEFGIFNQKICGGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGRVEHTS
QGAKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAKAPNDFNLKDFNVG
GYIQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDIIRR
FKSSKFGCRDPVRTNFDAFPDKVAIQLNDTHPSLAIPELMRVLVDLERLD
WDKAWEVTVKTCAYTNHTVIPEALERWPVHLLETLLPRHLQIIYEINQRF
LNRVAAAFPGDVDRLRRMSLVEEGAVKRINMAHLCIAGSHAVNGVARIHS
EILKKTIFKDFYELEPHKFQNKTNGITPRRWLVLCNPGLAEIIAERIGEE
YISDLDQLRKLLSYVDDEAFIRDVAKVKQENKLKFAAYLEREYKVHINPN
SLFDVQVKRIHEYKRQLLNCLHVITLYNRIKKEPNKFVVPRTVMIGGKAA
PGYHMAKMIIKLITAIGDVVNHDPVVGDRLRVIFLENYRVSLAEKVIPAA
DLSEQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENFFI
FGMRVEDVDRLDQRGYNAQEYYDRIPELRQIIEQLSSGFFSPKQPDLFKD
IVNMLMHHDRFKVFADYEEYVKCQERVSALYKNPREWTRMVIRNIATSGK
FSSDRTIAQYAREIWGVEPSRQRLPAPDEKIP
3D structure
PDB8gpb Structural mechanism for glycogen phosphorylase control by phosphorylation and AMP.
ChainA
Resolution2.2 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) H367 K558 R559 K564 T666 K670
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 G134 K568 Y648 R649 G675 T676 G677 K680 G124 K558 Y638 R639 G665 T666 G667 K670
BS02 AMP A Q72 Y75 R309 R310 Q62 Y65 R299 R300 MOAD: Kd=250uM
PDBbind-CN: -logKd/Ki=3.60,Kd=0.25mM
BS03 AMP A N282 F285 P611 G612 Y613 N272 F275 P601 G602 Y603 MOAD: Kd=250uM
PDBbind-CN: -logKd/Ki=3.60,Kd=0.25mM
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:8gpb, PDBe:8gpb, PDBj:8gpb
PDBsum8gpb
PubMed1900534
UniProtP00489|PYGM_RABIT Glycogen phosphorylase, muscle form (Gene Name=PYGM)

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