Structure of PDB 2ati Chain A

Receptor sequence
>2atiA (length=791) Species: 9606 (Homo sapiens) [Search protein sequence]
NVAELKKSFNRHLHFTLVKDRNVATTRDYYFALAHTVRDHLVGRWIRTQQ
HYYDKCPKRVYYLSLEFYMGRTLQNTMINLGLQNACDEAIYQLGLDIEEL
EEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEYGIFNQKIRD
GWQVEEADDWLRYGNPWEKSRPEFMLPVHFYGKVEHTNTGTKWIDTQVVL
ALPYDTPVPGYMNNTVNTMRLWSARAPDYIQAVLDRNLAENISRVLYPND
NFFEGKELRLKQEYFVVAATLQDIIRRFKASKFTVFDAFPDQVAIQLNDT
HPALAIPELMRIFVDIEKLPWSKAWELTQKTFAYTNHTVLPEALERWPVD
LVEKLLPRHLEIIYEINQKHLDRIVALFPKDVDRLRRMSLIEEEGSKRIN
MAHLCIVGSHAVNGVAKIHSDIVKTKVFKDFSELEPDKFQNKTNGITPRR
WLLLCNPGLAELIAEKIGEDYVKDLSQLTKLHSFLGDDVFLRELAKVKQE
NKLKFSQFLETEYKVKINPSSMFDVQVKRIHEYKRQLLNCLHVITMYNRI
KKDPKKLFVPRTVIIGGKAAPGYHMAKMIIKLITSVADVVNNDPMVGSKL
KVIFLENYRVSLAEKVIPATDLSEQISTAGTEASGTGNMKFMLNGALTIG
TMDGANVEMAEEAGEENLFIFGMRIDDVAALDKKGYEAKEYYEALPELKL
VIDQIDNGFFSPKQPDLFKDIINMLFYHDRFKVFADYEAYVKCQDKVSQL
YMNPKAWNTMVLKNIAASGKFSSDRTIKEYAQNIWNVEPSD
3D structure
PDB2ati Acyl ureas as human liver glycogen phosphorylase inhibitors for the treatment of type 2 diabetes.
ChainA
Resolution1.9 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) H337 K528 R529 K534 T636 K640
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 N284 H377 V455 N484 E672 A673 S674 G675 G113 L114 N251 H337 V415 N444 E632 A633 S634 G635
BS02 IHU A V40 K41 D42 N44 V45 V18 K19 D20 N22 V23 MOAD: ic50=23nM
BindingDB: IC50=23nM
BS03 PLP A Y90 G134 K568 Y648 R649 G675 T676 G677 K680 Y68 G112 K528 Y608 R609 G635 T636 G637 K640
BS04 IHU A W67 I68 Q71 Q72 K191 R193 W45 I46 Q49 Q50 K169 R171 MOAD: ic50=23nM
BindingDB: IC50=23nM
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:2ati, PDBe:2ati, PDBj:2ati
PDBsum2ati
PubMed16190745
UniProtP06737|PYGL_HUMAN Glycogen phosphorylase, liver form (Gene Name=PYGL)

[Back to BioLiP]