Structure of PDB 2qll Chain A

Receptor sequence
>2qllA (length=806) Species: 9606 (Homo sapiens) [Search protein sequence]
LTDQEKRRQISIRGIVGVENVAELKKSFNRHLHFTLVKDRNVATTRDYYF
ALAHTVRDHLVGRWIRTQQHYYDKCPKRVYYLSLEFYMGRTLQNTMINLG
LQNACDEAIYQLGLDIEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLA
AYGYGIRYFNQKIRDGWQVEEADDWLRYGNPWEKSRPEFMLPVHFYGKVE
HTNTGTKWIDTQVVLALPYDTPVPGYMNNTVNTMRLWSARAPNVLDRNLA
ENISRVLYPFEGKELRLKQEYFVVAATLQDIIRRFKASKFGTVFDAFPDQ
VAIQLNDTHPALAIPELMRIFVDIEKLPWSKAWELTQKTFAYTNHTVLPE
ALERWPVDLVEKLLPRHLEIIYEINQKHLDRIVALFPKDVDRLRRMSLIE
EEGSKRINMAHLCIVGSHAVNGVAKIHSDIVKTKVFKDFSELEPDKFQNK
TNGITPRRWLLLCNPGLAELIAEKIGEDYVKDLSQLTKLHSFLGDDVFLR
ELAKVKQENKLKFSQFLETEYKVKINPSSMFDVQVKRIHEYKRQLLNCLH
VITMYNRIKKDPKKLFVPRTVIIGGKAAPGYHMAKMIIKLITSVADVVNN
DPMVGSKLKVIFLENYRVSLAEKVIPATDLSEQISTAGTEASGTGNMKFM
LNGALTIGTMDGANVEMAEEAGEENLFIFGMRIDDVAALDKKGYEAKEYY
EALPELKLVIDQIDNGFFSPKQPDLFKDIINMLFYHDRFKVFADYEAYVK
CQDKVSQLYMNPKAWNTMVLKNIAASGKFSSDRTIKEYAQNIWNVEPSDL
KISLSN
3D structure
PDB2qll Molecular recognition of the protein phosphatase 1 glycogen targeting subunit by glycogen phosphorylase.
ChainA
Resolution2.56 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) H345 K536 R537 K542 T644 K648
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 peptide A Q71 Y75 Y155 F196 R242 D306 R309 R310 A313 Q68 Y72 Y152 F189 R235 D280 R283 R284 A287
BS02 PLP A Y90 G135 Y648 R649 V650 T676 K680 Y87 G132 Y616 R617 V618 T644 K648
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:2qll, PDBe:2qll, PDBj:2qll
PDBsum2qll
PubMed18198182
UniProtP06737|PYGL_HUMAN Glycogen phosphorylase, liver form (Gene Name=PYGL)

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