Structure of PDB 3mrx Chain A

Receptor sequence
>3mrxA (length=811) Species: 9986 (Oryctolagus cuniculus) [Search protein sequence]
QISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVATPRDYYFALAHTVRD
HLVGRWIRTQQHYYEKDPKRIYYLSLEFYMGRTLQNTMVNLALENACDEA
TYQLGLDMEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRY
EFGIFNQKICGGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGRVEHTSQ
GAKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAKAPNDFNLGGYIQAV
LDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDIIRRFKSSTN
FDAFPDKVAIQLNDTHPSLAIPELMRVLVDLERLDWDKAWEVTVKTCAYT
NHTVLPEALERWPVHLLETLLPRHLQIIYEINQRFLNRVAAAFPGDVDRL
RRMSLVEEGAVKRINMAHLCIAGSHAVNGVARIHSEILKKTIFKDFYELE
PHKFQNKTNGITPRRWLVLCNPGLAEIIAERIGEEYISDLDQLRKLLSYV
DDEAFIRDVAKVKQENKLKFAAYLEREYKVHINPNSLFDVQVKRIHEYKR
QLLNCLHVITLYNRIKKEPNKFVVPRTVMIGGKAAPGYHMAKMIIKLITA
IGDVVNHDPVVGDRLRVIFLENYRVSLAEKVIPAADLSEQISTAGTEASG
TGNMKFMLNGALTIGTMDGANVEMAEEAGEENFFIFGMRVEDVDRLDQRG
YNAQEYYDRIPELRQIIEQLSSGFFSPKQPDLFKDIVNMLMHHDRFKVFA
DYEEYVKCQERVSALYKNPREWTRMVIRNIATSGKFSSDRTIAQYAREIW
GVEPSRQRLPA
3D structure
PDB3mrx The binding of beta-D-glucopyranosyl-thiosemicarbazone derivatives to glycogen phosphorylase: a new class of inhibitors
ChainA
Resolution1.95 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) H352 K543 R544 K549 T651 K655
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 17S A R60 L63 W67 E190 K191 A192 P229 R49 L52 W56 E179 K180 A181 P218 MOAD: ic50=406.5uM
PDBbind-CN: -logKd/Ki=3.39,IC50=406.5uM
BS02 17S A E88 G135 L136 N282 D283 H341 H377 N484 E672 S674 G675 E77 G124 L125 N266 D267 H316 H352 N459 E647 S649 G650 MOAD: ic50=406.5uM
PDBbind-CN: -logKd/Ki=3.39,IC50=406.5uM
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:3mrx, PDBe:3mrx, PDBj:3mrx
PDBsum3mrx
PubMed20947361
UniProtP00489|PYGM_RABIT Glycogen phosphorylase, muscle form (Gene Name=PYGM)

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