Structure of PDB 1fa9 Chain A

Receptor sequence
>1fa9A (length=834) Species: 9606 (Homo sapiens) [Search protein sequence]
TDQEKRRQISIRGIVGVENVAELKKSFNRHLHFTLVKDRNVATTRDYYFA
LAHTVRDHLVGRWIRTQQHYYDKCPKRVYYLSLEFYMGRTLQNTMINLGL
QNACDEAIYQLGLDIEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAA
YGYGIRYEYGIFNQKIRDGWQVEEADDWLRYGNPWEKSRPEFMLPVHFYG
KVEHTNTGTKWIDTQVVLALPYDTPVPGYMNNTVNTMRLWSARAPNDFNL
RDFNVGDYIQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATL
QDIIRRFKASKFGSTRGAGTVFDAFPDQVAIQLNDTHPALAIPELMRIFV
DIEKLPWSKAWELTQKTFAYTNHTVLPEALERWPVDLVEKLLPRHLEIIY
EINQKHLDRIVALFPKDVDRLRRMSLIEEEGSKRINMAHLCIVGSHAVNG
VAKIHSDIVKTKVFKDFSELEPDKFQNKTNGITPRRWLLLCNPGLAELIA
EKIGEDYVKDLSQLTKLHSFLGDDVFLRELAKVKQENKLKFSQFLETEYK
VKINPSSMFDVQVKRIHEYKRQLLNCLHVITMYNRIKKDPKKLFVPRTVI
IGGKAAPGYHMAKMIIKLITSVADVVNNDPMVGSKLKVIFLENYRVSLAE
KVIPATDLSEQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAG
EENLFIFGMRIDDVAALDKKGYEAKEYYEALPELKLVIDQIDNGFFSPKQ
PDLFKDIINMLFYHDRFKVFADYEAYVKCQDKVSQLYMNPKAWNTMVLKN
IAASGKFSSDRTIKEYAQNIWNVEPSDLKISLSN
3D structure
PDB1fa9 Activation of human liver glycogen phosphorylase by alteration of the secondary structure and packing of the catalytic core.
ChainA
Resolution2.4 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) H373 K564 R565 K570 T672 K676
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 H377 N484 S674 G675 T676 G131 L132 H373 N480 S670 G671 T672
BS02 AMP A W67 Q71 Y75 R309 R310 W63 Q67 Y71 R305 R306
BS03 PLP A G135 W491 Y648 R649 V650 K680 G131 W487 Y644 R645 V646 K676
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0002060 purine nucleobase binding
GO:0004645 1,4-alpha-oligoglucan phosphorylase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0005536 D-glucose binding
GO:0008184 glycogen phosphorylase activity
GO:0016208 AMP binding
GO:0016757 glycosyltransferase activity
GO:0019842 vitamin binding
GO:0030170 pyridoxal phosphate binding
GO:0030246 carbohydrate binding
GO:0032052 bile acid binding
GO:0042802 identical protein binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0005977 glycogen metabolic process
GO:0005980 glycogen catabolic process
GO:0006015 5-phosphoribose 1-diphosphate biosynthetic process
GO:0009617 response to bacterium
GO:0042593 glucose homeostasis
GO:0070266 necroptotic process
Cellular Component
GO:0005576 extracellular region
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0034774 secretory granule lumen
GO:0070062 extracellular exosome
GO:1904813 ficolin-1-rich granule lumen

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1fa9, PDBe:1fa9, PDBj:1fa9
PDBsum1fa9
PubMed10949035
UniProtP06737|PYGL_HUMAN Glycogen phosphorylase, liver form (Gene Name=PYGL)

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