Structure of PDB 1l7x Chain A

Receptor sequence
>1l7xA (length=793) Species: 9606 (Homo sapiens) [Search protein sequence]
ENVAELKKSFNRHLHFTLVKDRNVATTRDYYFALAHTVRDHLVGRWIRTQ
QHYYDKCPKRVYYLSLEFYMGRTLQNTMINLGLQNACDEAIYQLGLDIEE
LEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEYGIFNQKIR
DGWQVEEADDWLRYGNPWEKSRPEFMLPVHFYGKVEHTNTGTKWIDTQVV
LALPYDTPVPGYMNNTVNTMRLWSARAPNDGDYIQAVLDRNLAENISRVL
YPNDNFFEGKELRLKQEYFVVAATLQDIIRRFKASKFTVFDAFPDQVAIQ
LNDTHPALAIPELMRIFVDIEKLPWSKAWELTQKTFAYTNHTVLPEALER
WPVDLVEKLLPRHLEIIYEINQKHLDRIVALFPKDVDRLRRMSLIEEEGS
KRINMAHLCIVGSHAVNGVAKIHSDIVKTKVFKDFSELEPDKFQNKTNGI
TPRRWLLLCNPGLAELIAEKIGEDYVKDLSQLTKLHSFLGDDVFLRELAK
VKQENKLKFSQFLETEYKVKINPSSMFDVQVKRIHEYKRQLLNCLHVITM
YNRIKKDPKKLFVPRTVIIGGKAAPGYHMAKMIIKLITSVADVVNNDPMV
GSKLKVIFLENYRVSLAEKVIPATDLSEQISTAGTEASGTGNMKFMLNGA
LTIGTMDGANVEMAEEAGEENLFIFGMRIDDVAALDKKGYEAKEYYEALP
ELKLVIDQIDNGFFSPKQPDLFKDIINMLFYHDRFKVFADYEAYVKCQDK
VSQLYMNPKAWNTMVLKNIAASGKFSSDRTIKEYAQNIWNVEP
3D structure
PDB1l7x Structure-activity analysis of the purine binding site of human liver glycogen phosphorylase.
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) H341 K532 R533 K538 T640 K644
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 NBG A N284 H377 V455 N484 E672 S674 G675 N255 H341 V419 N448 E636 S638 G639
BS02 PLP A Y648 R649 G675 T676 K680 Y612 R613 G639 T640 K644
BS03 700 A R60 W67 P188 E190 K191 S192 R39 W46 P167 E169 K170 S171 MOAD: ic50=0.145uM
BindingDB: IC50=45nM
BS04 CFF A F285 H571 A610 G612 Y613 F256 H535 A574 G576 Y577 MOAD: Kd=92uM
PDBbind-CN: -logKd/Ki=4.04,Kd=92uM
BS05 CFF A W174 H614 W153 H578 MOAD: Kd=92uM
PDBbind-CN: -logKd/Ki=4.04,Kd=92uM
BS06 700 A T38 V40 F53 H57 P188 T17 V19 F32 H36 P167 MOAD: ic50=0.145uM
BindingDB: IC50=45nM
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:1l7x, PDBe:1l7x, PDBj:1l7x
PDBsum1l7x
PubMed12204691
UniProtP06737|PYGL_HUMAN Glycogen phosphorylase, liver form (Gene Name=PYGL)

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