Structure of PDB 1l7x Chain B

Receptor sequence
>1l7xB (length=795) Species: 9606 (Homo sapiens) [Search protein sequence]
GVENVAELKKSFNRHLHFTLVKDRNVATTRDYYFALAHTVRDHLVGRWIR
TQQHYYDKCPKRVYYLSLEFYMGRTLQNTMINLGLQNACDEAIYQLGLDI
EELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEYGIFNQK
IRDGWQVEEADDWLRYGNPWEKSRPEFMLPVHFYGKVEHTNTGTKWIDTQ
VVLALPYDTPVPGYMNNTVNTMRLWSARAPNDGDYIQAVLDRNLAENISR
VLYPNDNFFEGKELRLKQEYFVVAATLQDIIRRFKASKFVFDAFPDQVAI
QLNDTHPALAIPELMRIFVDIEKLPWSKAWELTQKTFAYTNHTVLPEALE
RWPVDLVEKLLPRHLEIIYEINQKHLDRIVALFPKDVDRLRRMSLIEEEG
SKRINMAHLCIVGSHAVNGVAKIHSDIVKTKVFKDFSELEPDKFQNKTNG
ITPRRWLLLCNPGLAELIAEKIGEDYVKDLSQLTKLHSFLGDDVFLRELA
KVKQENKLKFSQFLETEYKVKINPSSMFDVQVKRIHEYKRQLLNCLHVIT
MYNRIKKDPKKLFVPRTVIIGGKAAPGYHMAKMIIKLITSVADVVNNDPM
VGSKLKVIFLENYRVSLAEKVIPATDLSEQISTAGTEASGTGNMKFMLNG
ALTIGTMDGANVEMAEEAGEENLFIFGMRIDDVAALDKKGYEAKEYYEAL
PELKLVIDQIDNGFFSPKQPDLFKDIINMLFYHDRFKVFADYEAYVKCQD
KVSQLYMNPKAWNTMVLKNIAASGKFSSDRTIKEYAQNIWNVEPS
3D structure
PDB1l7x Structure-activity analysis of the purine binding site of human liver glycogen phosphorylase.
ChainB
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) H342 K533 R534 K539 T641 K645
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 700 B T38 V40 F53 H57 P188 T19 V21 F34 H38 P169 MOAD: ic50=0.145uM
BindingDB: IC50=45nM
BS02 NBG B G135 L136 N284 H377 T378 N484 E672 S674 G675 G116 L117 N257 H342 T343 N449 E637 S639 G640
BS03 PLP B G134 G135 K568 K574 Y648 R649 V650 G675 T676 G677 K680 G115 G116 K533 K539 Y613 R614 V615 G640 T641 G642 K645
BS04 700 B R60 V64 W67 P188 W189 E190 K191 R41 V45 W48 P169 W170 E171 K172 MOAD: ic50=0.145uM
BindingDB: IC50=45nM
BS05 CFF B F285 H571 A610 G612 Y613 F258 H536 A575 G577 Y578 MOAD: Kd=92uM
PDBbind-CN: -logKd/Ki=4.04,Kd=92uM
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
View graph for
Cellular Component
External links
PDB RCSB:1l7x, PDBe:1l7x, PDBj:1l7x
PDBsum1l7x
PubMed12204691
UniProtP06737|PYGL_HUMAN Glycogen phosphorylase, liver form (Gene Name=PYGL)

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