Structure of PDB 1axr Chain A

Receptor sequence
>1axrA (length=829) Species: 9986 (Oryctolagus cuniculus) [Search protein sequence]
SVRGLAGVENVTELKKNFNRHLHFTLVKDRNVATPRDYYFALAHTVRDHL
VGRWIRTQQHYYEKDPKRIYYLSLEFYMGRTLQNTMVNLALENACDEATY
QLGLDMEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEF
GIFNQKICGGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGRVEHTSQGA
KWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAKAPNDFNLKDFNVGGYI
QAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDIIRRFKS
SKFGCRDPVRTNFDAFPDKVAIQLNDTHPSLAIPELMRVLVDLERLDWDK
AWEVTVKTCAYTNHTVLPEALERWPVHLLETLLPRHLQIIYEINQRFLNR
VAAAFPGDVDRLRRMSLVEEGAVKRINMAHLCIAGSHAVNGVARIHSEIL
KKTIFKDFYELEPHKFQNKTNGITPRRWLVLCNPGLAEIIAERIGEEYIS
DLDQLRKLLSYVDDEAFIRDVAKVKQENKLKFAAYLEREYKVHINPNSLF
DVQVKRIHEYKRQLLNCLHVITLYNRIKKEPNKFVVPRTVMIGGKAAPGY
HMAKMIIKLITAIGDVVNHDPVVGDRLRVIFLENYRVSLAEKVIPAADLS
EQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENFFIFGM
RVEDVDRLDQRGYNAQEYYDRIPELRQIIEQLSSGFFSPKQPDLFKDIVN
MLMHHDRFKVFADYEEYVKCQERVSALYKNPREWTRMVIRNIATSGKFSS
DRTIAQYAREIWGVEPSRQRLPAPDEKIP
3D structure
PDB1axr ?
ChainA
Resolution2.3 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) H364 K555 R556 K561 T663 K667
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 PLP A Y90 G134 K568 Y648 G675 T676 G677 K680 Y77 G121 K555 Y635 G662 T663 G664 K667
BS02 HTP A L136 L139 N284 H377 N484 E672 S674 G675 L123 L126 N271 H364 N471 E659 S661 G662 MOAD: Ki=540uM
PDBbind-CN: -logKd/Ki=3.27,Ki=540uM
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1axr, PDBe:1axr, PDBj:1axr
PDBsum1axr
PubMed
UniProtP00489|PYGM_RABIT Glycogen phosphorylase, muscle form (Gene Name=PYGM)

[Back to BioLiP]