Structure of PDB 1hlf Chain A

Receptor sequence
>1hlfA (length=830) Species: 9986 (Oryctolagus cuniculus) [Search protein sequence]
ISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVATPRDYYFALAHTVRDH
LVGRWIRTQQHYYEKDPKRIYYLSLEFYMGRTLQNTMVNLALENACDEAT
YQLGLDMEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYE
FGIFNQKICGGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGRVEHTSQG
AKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAKAPNDFNLKDFNVGGY
IQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDIIRRFK
SSKFGCRDPVRTNFDAFPDKVAIQLNDTHPSLAIPELMRVLVDLERLDWD
KAWEVTVKTCAYTNHTVIPEALERWPVHLLETLLPRHLQIIYEINQRFLN
RVAAAFPGDVDRLRRMSLVEEGAVKRINMAHLCIAGSHAVNGVARIHSEI
LKKTIFKDFYELEPHKFQNKTNGITPRRWLVLCNPGLAEIIAERIGEEYI
SDLDQLRKLLSYVDDEAFIRDVAKVKQENKLKFAAYLEREYKVHINPNSL
FDVQVKRIHEYKRQLLNCLHVITLYNRIKKEPNKFVVPRTVMIGGKAAPG
YHMAKMIIKLITAIGDVVNHDPVVGDRLRVIFLENYRVSLAEKVIPAADL
SEQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENFFIFG
MRVEDVDRLDQRGYNAQEYYDRIPELRQIIEQLSSGFFSPKQPDLFKDIV
NMLMHHDRFKVFADYEEYVKCQERVSALYKNPREWTRMVIRNIATSGKFS
SDRTIAQYAREIWGVEPSRQRLPAPDEKIP
3D structure
PDB1hlf Kinetic and crystallographic studies of glucopyranosylidene spirothiohydantoin binding to glycogen phosphorylase B
ChainA
Resolution2.26 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) H365 K556 R557 K562 T664 K668
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 G134 K568 Y648 R649 V650 G675 T676 G677 K680 G122 K556 Y636 R637 V638 G663 T664 G665 K668
BS02 GL4 A G135 L136 N284 H377 N484 E672 G675 G123 L124 N272 H365 N472 E660 G663 MOAD: Ki=2.3uM
PDBbind-CN: -logKd/Ki=5.64,Ki=2.3uM
BindingDB: Ki=5100nM
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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Biological Process
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Cellular Component
External links
PDB RCSB:1hlf, PDBe:1hlf, PDBj:1hlf
PDBsum1hlf
PubMed11741774
UniProtP00489|PYGM_RABIT Glycogen phosphorylase, muscle form (Gene Name=PYGM)

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