Structure of PDB 1exv Chain A

Receptor sequence
>1exvA (length=786) Species: 9606 (Homo sapiens) [Search protein sequence]
NVAELKKSFNRHLHFTLVKDRNVATTRDYYFALAHTVRDHLVGRWIRTQQ
HYYDKCPKRVYYLSLEFYMGRTLQNTMINLGLQNACDEAIYQLGLDIEEL
EEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEYGIFNQKIRD
GWQVEEADDWLRYGNPWEKSRPEFMLPVHFYGKVEHTNTGTKWIDTQVVL
ALPYDTPVPGYMNNTVNTMRLWSARAPGDYIQAVLDRNLAENISRVLYPN
DNFFEGKELRLKQEYFVVAATLQDIIRRFKAFDAFPDQVAIQLNDTHPAL
AIPELMRIFVDIEKLPWSKAWELTQKTFAYTNHTVLPEALERWPVDLVEK
LLPRHLEIIYEINQKHLDRIVALFPKDVDRLRRMSLIEEEGSKRINMAHL
CIVGSHAVNGVAKIHSDIVKTKVFKDFSELEPDKFQNKTNGITPRRWLLL
CNPGLAELIAEKIGEDYVKDLSQLTKLHSFLGDDVFLRELAKVKQENKLK
FSQFLETEYKVKINPSSMFDVQVKRIHEYKRQLLNCLHVITMYNRIKKDP
KKLFVPRTVIIGGKAAPGYHMAKMIIKLITSVADVVNNDPMVGSKLKVIF
LENYRVSLAEKVIPATDLSEQISTAGTEASGTGNMKFMLNGALTIGTMDG
ANVEMAEEAGEENLFIFGMRIDDVAALDKKGYEAKEYYEALPELKLVIDQ
IDNGFFSPKQPDLFKDIINMLFYHDRFKVFADYEAYVKCQDKVSQLYMNP
KAWNTMVLKNIAASGKFSSDRTIKEYAQNIWNVEPS
3D structure
PDB1exv Human liver glycogen phosphorylase inhibitors bind at a new allosteric site.
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) H377 K568 R569 K574 T676 K680
Catalytic site (residue number reindexed from 1) H333 K524 R525 K530 T632 K636
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 N484 E672 S674 G675 N252 H333 N440 E628 S630 G631
BS02 PLP A Y90 G134 G135 K568 Y648 R649 V650 G675 T676 G677 K680 Y68 G112 G113 K524 Y604 R605 V606 G631 T632 G633 K636
BS03 700 A R60 W67 P188 E190 K191 R38 W45 P166 E168 K169 MOAD: ic50=45nM
PDBbind-CN: -logKd/Ki=7.35,IC50=45nM
BindingDB: IC50=45nM
BS04 700 A T38 V40 F53 H57 P188 T16 V18 F31 H35 P166 MOAD: ic50=45nM
PDBbind-CN: -logKd/Ki=7.35,IC50=45nM
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1exv, PDBe:1exv, PDBj:1exv
PDBsum1exv
PubMed10980448
UniProtP06737|PYGL_HUMAN Glycogen phosphorylase, liver form (Gene Name=PYGL)

[Back to BioLiP]