Structure of PDB 1noi Chain A

Receptor sequence
>1noiA (length=823) Species: 9986 (Oryctolagus cuniculus) [Search protein sequence]
RKQISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVATPRDYYFALAHTV
RDHLVGRWIRTQQHYYEKDPKRIYYLSLEFYMGRTLQNTMVNLALENACD
EATYQLGLDMEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGI
RYEFGIFNQKICGGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGRVEHT
SQGAKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAKAPNDFNLKDFNV
GGYIQAVLDRNLAENISRVLYPEGKELRLKQEYFVVAATLQDIIRRFKSS
KFGCRDPVRTNFDAFPDKVAIQLNDTHPSLAIPELMRVLVDLERLDWDKA
WEVTVKTCAYTNHTVIPEALERWPVHLLETLLPRHLQIIYEINQRFLNRV
AAAFPGDVDRLRRMSLVEEGAVKRINMAHLCIAGSHAVNGVARIHSEILK
KTIFKDFYELEPHKFQNKTNGITPRRWLVLCNPGLAEIIAERIGEEYISD
LDQLRKLLSYVDDEAFIRDVAKVKQENKLKFAAYLEREYKVHINPNSLFD
VQVKRIHEYKRQLLNCLHVITLYNRIKKEPNKFVVPRTVMIGGKPAPGYH
MAKMIIKLITAIGDVVNHDPVVGDRLRVIFLENYRVSLAEKVIPAADLSE
QISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENFFIFGMR
VEDVDRLDQRGYNAQEYYDRIPELRQIIEQLSSGFFSPKQPDLFKDIVNM
LMHHDRFKVFADYEEYVKCQERVSALYKNPREWTRMVIRNIATSGKFSSD
RTIAQYAREIWGVEPSRQRLPAP
3D structure
PDB1noi Ternary complex crystal structures of glycogen phosphorylase with the transition state analogue nojirimycin tetrazole and phosphate in the T and R states.
ChainA
Resolution2.5 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) H363 K554 R555 K560 T662 K666
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 PO4 A G135 R569 K574 G126 R555 K560
BS02 PLP A K568 Y648 V650 G675 T676 G677 K680 K554 Y634 V636 G661 T662 G663 K666
BS03 NTZ A L136 H377 T378 N484 E672 G675 L127 H363 T364 N470 E658 G661 MOAD: Ki=700uM
PDBbind-CN: -logKd/Ki=3.15,Ki=700uM
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:1noi, PDBe:1noi, PDBj:1noi
PDBsum1noi
PubMed8652510
UniProtP00489|PYGM_RABIT Glycogen phosphorylase, muscle form (Gene Name=PYGM)

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