Structure of PDB 1z8d Chain A

Receptor sequence
>1z8dA (length=821) Species: 9606 (Homo sapiens) [Search protein sequence]
RPLSDQEKRKQISVRGVENVTELKKNFNRHLHFTLVKDRNVATPRDYYFA
LAHTVRDHLVGRWIRTQQHYYEKDPKRIYYLSLEFYMGRTLQNTMVNLAL
ENACDEATYQLGLDMEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAA
YGYGIRYEFGIFNQKISGGWQMEEADDWLRYGNPWEKARPEFTLPVHFYG
HVEHTSQGAKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAKAPGYIQA
VLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDIIRRFKSSK
FGCRDPVRTNFDAFPDKVAIQLNDTHPSLAIPELMRILVDLERMDWDKAW
DVTVRTCAYTNHTVLPEALERWPVHLLETLLPRHLQIIYEINQRFLNRVA
AAFPGDVDRLRRMSLVEEGAVKRINMAHLCIAGSHAVNGVARIHSEILKK
TIFKDFYELEPHKFQNKTNGITPRRWLVLCNPGLAEVIAERIGEDFISDL
DQLRKLLSFVDDEAFIRDVAKVKQENKLKFAAYLEREYKVHINPNSLFDI
QVKRIHEYKRQLLNCLHVITLYNRIKREPNKFFVPRTVMIGGKAAPGYHM
AKMIIRLVTAIGDVVNHDPAVGDRLRVIFLENYRVSLAEKVIPAADLSEQ
ISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENFFIFGMRV
EDVDKLDQRGYNAQEYYDRIPELRQVIEQLSSGFFSPKQPDLFKDIVNML
MHHDRFKVFADYEDYIKCQEKVSALYKNPREWTRMVIRNIATSGKFSSDR
TIAQYAREIWGVEPSRQRLPA
3D structure
PDB1z8d The crystal structure of human muscle glycogen phosphorylase a with bound glucose and AMP: An intermediate conformation with T-state and R-state features.
ChainA
Resolution2.3 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) H362 K553 R554 K559 T661 K665
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 GLC A G135 L136 L139 N284 H377 V455 N484 E672 S674 G675 G131 L132 L135 N269 H362 V440 N469 E657 S659 G660
BS02 AMP A W67 Q71 Y75 R309 R310 F316 G317 C318 W63 Q67 Y71 R294 R295 F301 G302 C303
BS03 ADE A F285 G612 Y613 F270 G597 Y598
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004645 1,4-alpha-oligoglucan phosphorylase activity
GO:0005515 protein binding
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:0005829 cytosol
GO:0070062 extracellular exosome

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1z8d, PDBe:1z8d, PDBj:1z8d
PDBsum1z8d
PubMed16523484
UniProtP11217|PYGM_HUMAN Glycogen phosphorylase, muscle form (Gene Name=PYGM)

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