Structure of PDB 1a8i Chain A

Receptor sequence
>1a8iA (length=813) Species: 9986 (Oryctolagus cuniculus) [Search protein sequence]
QEKRKQISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVATPRDYYFALA
HTVRDHLVGRWIRTQQHYYEKDPKRIYYLSLEFYMGRTLQNTMVNLALEN
ACDEATYQLGLDMEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYG
YGIRYEFGIFNQKICGGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGRV
EHTSQGAKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAKAPNGYIQAV
LDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDIIRRFKSSKF
RTNFDAFPDKVAIQLNDTHPSLAIPELMRVLVDLERLDWDKAWEVTVKTC
AYTNHTVIPEALERWPVHLLETLLPRHLQIIYEINQRFLNRVAAAFPGDV
DRLRRMSLVEEGAVKRINMAHLCIAGSHAVNGVARIHSEILKKTIFKDFY
ELEPHKFQNKTNGITPRRWLVLCNPGLAEIIAERIGEEYISDLDQLRKLL
SYVDDEAFIRDVAKVKQENKLKFAAYLEREYKVHINPNSLFDVQVKRIHE
YKRQLLNCLHVITLYNRIKKEPNKFVVPRTVMIGGKAAPGYHMAKMIIKL
ITAIGDVVNHDPVVGDRLRVIFLENYRVSLAEKVIPAADLSEQISTAGTE
ASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENFFIFGMRVEDVDRLD
QRGYNAQEYYDRIPELRQIIEQLSSGFFSPKQPDLFKDIVNMLMHHDRFK
VFADYEEYVKCQERVSALYKNPREWTRMVIRNIATSGKFSSDRTIAQYAR
EIWGVEPSRQRLP
3D structure
PDB1a8i The structure of a glycogen phosphorylase glucopyranose spirohydantoin complex at 1.8 A resolution and 100 K: the role of the water structure and its contribution to binding.
ChainA
Resolution1.78 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) H355 K546 R547 K552 T654 K658
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 GLS A G135 L136 N284 H377 V455 N484 E672 S674 G675 G129 L130 N268 H355 V433 N462 E650 S652 G653 MOAD: Ki=3uM
PDBbind-CN: -logKd/Ki=5.52,Ki=3.0uM
BindingDB: Ki=3100nM,IC50=3100nM
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004645 1,4-alpha-oligoglucan phosphorylase activity
GO:0008184 glycogen phosphorylase activity
GO:0016757 glycosyltransferase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0005977 glycogen metabolic process
GO:0005980 glycogen catabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0098723 skeletal muscle myofibril

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Molecular Function
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Cellular Component
External links
PDB RCSB:1a8i, PDBe:1a8i, PDBj:1a8i
PDBsum1a8i
PubMed9568898
UniProtP00489|PYGM_RABIT Glycogen phosphorylase, muscle form (Gene Name=PYGM)

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