Structure of PDB 2qn7 Chain A

Receptor sequence
>2qn7A (length=805) Species: 9986 (Oryctolagus cuniculus) [Search protein sequence]
ISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVATPRDYYFALAHTVRDH
LVGRWIRTQQHYYEKDPKRIYYLSLEFYMGRTLQNTMVNLALENACDEAT
YQLGLDMEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYE
FGIFNQKICGGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGRVEHTSQG
AKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAKAPNDGYIQAVLDRNL
AENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDIIRRFKSSNFDAFPD
KVAIQLNDTHPSLAIPELMRVLVDLERLDWDKAWEVTVKTCAYTNHTVIP
EALERWPVHLLETLLPRHLQIIYEINQRFLNRVAAAFPGDVDRLRRMSLV
EEGAVKRINMAHLCIAGSHAVNGVARIHSEILKKTIFKDFYELEPHKFQN
KTNGITPRRWLVLCNPGLAEIIAERIGEEYISDLDQLRKLLSYVDDEAFI
RDVAKVKQENKLKFAAYLEREYKVHINPNSLFDVQVKRIHEYKRQLLNCL
HVITLYNRIKKEPNKFVVPRTVMIGGKAAPGYHMAKMIIKLITAIGDVVN
HDPVVGDRLRVIFLENYRVSLAEKVIPAADLSEQISTAGTEASGTGNMKF
MLNGALTIGTMDGANVEMAEEAGEENFFIFGMRVEDVDRLDQRGYNAQEY
YDRIPELRQIIEQLSSGFFSPKQPDLFKDIVNMLMHHDRFKVFADYEEYV
KCQERVSALYKNPREWTRMVIRNIATSGKFSSDRTIAQYAREIWGVEPSR
QRLPA
3D structure
PDB2qn7 N-(4-substituted-benzoyl)-N'-(beta-D-glucopyranosyl)ureas, inhibitors of glycogen phosphorylase: synthesis, kinetic and crystallographic evaluation
ChainA
Resolution1.83 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) H346 K537 R538 K543 T645 K649
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 G135 K568 Y648 R649 G675 T676 G677 K680 G122 G123 K537 Y617 R618 G644 T645 G646 K649
BS02 HBZ A E88 G135 L136 N282 D283 H341 H377 N484 E672 A673 S674 G675 E76 G123 L124 N261 D262 H310 H346 N453 E641 A642 S643 G644 BindingDB: Ki=6300nM
BS03 IMP A Y75 R309 R310 Y63 R288 R289
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:2qn7, PDBe:2qn7, PDBj:2qn7
PDBsum2qn7
PubMed
UniProtP00489|PYGM_RABIT Glycogen phosphorylase, muscle form (Gene Name=PYGM)

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