3L01: GlgA glycogen synthase

Crystal structure of monomeric glycogen synthase from Pyrococcus abyssi. Determined by X-ray diffraction at 2.6 Å resolution. Released 29 Dec 2010.

Method
X-ray diffraction
Resolution
2.6 Å
Organism
Pyrococcus abyssi
Chains
2
Atoms
7,011
Mol. weight
98.3 kDa
Released
29 Dec 2010

Explore 3L01 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3L01 contains 49 α-helices and 42 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 25 helices, 21 β-strands

ElementResiduesLengthSheet
β-strand2-651
β-strand1012
β-strand1312
α-helix18-3114
β-strand35-4171
β-strand49-5681
β-strand59-70121
β-strand73-7971
α-helix81-844
α-helix92-11524
α-helix119-1213
β-strand123-12751
α-helix129-1313
α-helix132-14211
β-strand146-15051
β-strand158-15923
α-helix161-1655
α-helix169-1713
β-strand176-17723
α-helix179-1868
β-strand189-19241
α-helix195-2006
α-helix202-2054
α-helix206-2083
β-strand212-21431
α-helix226-2283
α-helix233-24210
β-strand250-25564
β-strand25815
α-helix265-27511
α-helix280-2834
β-strand284-28964
β-strand29215
α-helix294-30613
β-strand310-31344
α-helix316-3183
α-helix319-3268
β-strand331-33444
α-helix343-3508
α-helix3531
β-strand354-35854
α-helix362-3665
β-strand373-37534
α-helix380-39314
α-helix398-40912
α-helix414-42512
Chain B: 24 helices, 21 β-strands
ElementResiduesLengthSheet
β-strand2-656
β-strand1017
β-strand1317
α-helix18-3114
β-strand35-4176
β-strand49-5686
β-strand59-70126
β-strand73-7976
α-helix81-844
α-helix92-11524
α-helix119-1213
β-strand123-12756
α-helix129-1313
α-helix132-14211
β-strand146-15056
β-strand158-15928
α-helix161-1655
α-helix169-1713
β-strand176-17728
α-helix179-1868
β-strand189-19246
α-helix195-2006
α-helix202-2054
α-helix206-2083
β-strand212-21436
α-helix226-2283
α-helix233-24210
β-strand250-25569
β-strand258110
α-helix265-27511
α-helix279-2824
β-strand284-28969
β-strand292110
α-helix294-30613
β-strand310-31349
α-helix319-3268
β-strand331-33449
α-helix343-3508
α-helix3531
β-strand354-35859
α-helix363-3664
β-strand373-37539
α-helix380-39314
α-helix398-40912
α-helix414-42512

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
GlgA glycogen synthaseA, Bprotein428Pyrococcus abyssiQ9V2J8 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>3L01_1 GlgA glycogen synthase (chains A, B)
RHMKVLLLGFEFLPVKVGGLAEALTAISEALASLGHEVLVFTPSHGRFQGEEIGKIRVFG
EEVQVKVSYEERGNLRIYRIGGGLLDSEDVYGPGWDGLIRKAVTFGRASVLLLNDLLREE
PLPDVVHFHDWHTVFAGALIKKYFKIPAVFTIHRLNKSKLPAFYFHEAGLSELAPYPDID
PEHTGGYIADIVTTVSRGYLIDEWGFFRNFEGKITYVFNGIDCSFWNESYLTGSRDERKK
SLLSKFGMDEGVTFMFIGRFDRGQKGVDVLLKAIEILSSKKEFQEMRFIIIGKGDPELEG
WARSLEEKHGNVKVITEMLSREFVRELYGSVDFVIIPSYFEPFGLVALEAMCLGAIPIAS
AVGGLRDIITNETGILVKAGDPGELANAILKALELSRSDLSKFRENCKKRAMSFSWEKSA
ERYVKAYA

Primary citation

Processivity and Subcellular Localization of Glycogen Synthase Depend on a Non-catalytic High Affinity Glycogen-binding Site. Diaz, A., Martinez-Pons, C., Fita, I. et al. J Biol Chem (2011) 286:18505-18514. DOI 10.1074/jbc.M111.236109 · PubMed

Other PDB entries of the same protein (UniProt Q9V2J8 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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