Structure of PDB 3e3n Chain C

Receptor sequence
>3e3nC (length=802) Species: 9986 (Oryctolagus cuniculus) [Search protein sequence]
KRKQISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVATPRDYYFALAHT
VRDHLVGRWIRTQQHYYEKDPKRIYYLSLEFYMGRTLQNTMVNLALENAC
DEATYQLGLDMEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYG
IRYEFGIFNQKICGGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGRVEH
TSQGAKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAKAPNGYIQAVLD
RNLAENISRVLYGKELRLKQEYFVVAATLQDIIRRFKSSNFDAFPDKVAI
QLNDTHPSLAIPELMRVLVDLERLDWDKAWEVTVKTCAYTNHTVLPEALE
RWPVHLLETLLPRHLQIIYEINQRFLNRVAAAFPGDVDRLRRMSLVEEGA
VKRINMAHLCIAGSHAVNGVARIHSEILKKTIFKDFYELEPHKFQNKTNG
ITPRRWLVLCNPGLAEIIAERIGEEYISDLDQLRKLLSYVDDEAFIRDVA
KVKQENKLKFAAYLEREYKVHINPNSLFDVQVKRIHEYKRQLLNCLHVIT
LYNRIKKEPNKFVVPRTVMIGGKAAPGYHMAKMIIKLITAIGDVVNHDPV
VGDRLRVIFLENYRVSLAEKVIPAADLSEQISTAGTEASGTGNMKFMLNG
ALTIGTMDGANVEMAEEAGEENFFIFGMRVEDVDRLDQRGYNAQEYYDRI
PELRQIIEQLSSGFFSPKQPDLFKDIVNMLMHHDRFKVFADYEEYVKCQE
RVSALYKNPREWTRMVIRNIATSGKFSSDRTIAQYAREIWGVEPSRQRLP
AP
3D structure
PDB3e3n Glycogen phosphorylase revisited: extending the resolution of the R- and T-state structures of the free enzyme and in complex with allosteric activators.
ChainC
Resolution2.7 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) H342 K533 R534 K539 T641 K645
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 AMP C W67 Q71 Y75 R309 R310 W59 Q63 Y67 R284 R285
BS02 AMP C D42 N44 V45 D34 N36 V37
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:3e3n, PDBe:3e3n, PDBj:3e3n
PDBsum3e3n
PubMed34473107
UniProtP00489|PYGM_RABIT Glycogen phosphorylase, muscle form (Gene Name=PYGM)

[Back to BioLiP]