1WW3: Glycogen phosphorylase, muscle form

Crystallographic studies on two bioisosteric analogues, N-acetyl-beta-D-glucopyranosylamine and N-trifluoroacetyl-beta-D-glucopyranosylamine, potent inhibitors of muscle glycogen phosphorylase. Determined by X-ray diffraction at 1.8 Å resolution. Released 13 Dec 2005.

Method: X-ray diffraction
Resolution: 1.8 Å
Organism: Oryctolagus cuniculus
Chains: 1
Atoms: 7,015
Mol. weight: 97.81 kDa
Ligands: PLP, NTF
Released: 13 Dec 2005

Explore 1WW3 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1WW3 contains 54 α-helices and 29 β-strands across 1 chain. 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: 54 helices, 29 β-strands

Element	Residues	Length	Sheet
α-helix	14-16	3
α-helix	23-33	11
α-helix	34-38	5
α-helix	48-77	30
β-strand	81-85	5	1
β-strand	89-92	4	2
α-helix	95-102	8
α-helix	105-114	10
α-helix	119-123	5
α-helix	127-128	2
β-strand	129-131	3	2
α-helix	135-149	15
β-strand	154-159	6	1
β-strand	163	1	3
α-helix	166	1
β-strand	167-171	5	4
β-strand	174-178	5	4
β-strand	191-192	2	1
α-helix	194-196	3
β-strand	198-202	5	1
β-strand	205-209	5	5
β-strand	212-216	5	5
β-strand	219-231	13	1
β-strand	238-247	10	1
α-helix	262-267	6
α-helix	270-273	4
α-helix	274-276	3
β-strand	278	1	3
α-helix	290-311	22
α-helix	326-328	3
α-helix	329-332	4
β-strand	333-338	6	1
α-helix	345-351	7
α-helix	352-356	5
α-helix	361-371	11
β-strand	372-375	4	1
α-helix	381-383	3
β-strand	386-388	3	6
α-helix	389-395	7
α-helix	397-417	21
α-helix	422-428	7
β-strand	431-432	2	6
α-helix	433	1
β-strand	438-440	3	6
α-helix	441-447	7
β-strand	452-454	3	1
α-helix	457-465	9
α-helix	469-474	6
α-helix	476-478	3
β-strand	479-481	3	1
β-strand	486	1	7
α-helix	489-494	6
α-helix	497-507	11
α-helix	510-513	4
α-helix	515-524	10
α-helix	528-551	24
β-strand	562-567	6	8
α-helix	572-574	3
α-helix	576-592	17
β-strand	601-606	6	8
α-helix	614-630	17
β-strand	640-645	6	8
α-helix	650-656	7
α-helix	657-659	3
β-strand	662-665	4	8
α-helix	667-668	2
α-helix	677-683	7
β-strand	687-690	4	8
α-helix	696-703	8
α-helix	705-707	3
β-strand	709-710	2	8
α-helix	715-724	10
α-helix	728-734	7
α-helix	736-747	12
α-helix	759-767	9
α-helix	774-776	3
α-helix	777-791	15
α-helix	794-806	13
α-helix	809-811	3
β-strand	812	1	7
α-helix	813-820	8
α-helix	821-825	5
α-helix	832-834	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Glycogen phosphorylase, muscle form	A	protein	842	Oryctolagus cuniculus	P00489 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1WW3_1 Glycogen phosphorylase, muscle form (chains A)
SRPLSDQEKRKQISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVATPRDYYFALAHTVR
DHLVGRWIRTQQHYYEKDPKRIYYLSLEFYMGRTLQNTMVNLALENACDEATYQLGLDME
ELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQKICGGWQMEEAD
DWLRYGNPWEKARPEFTLPVHFYGRVEHTSQGAKWVDTQVVLAMPYDTPVPGYRNNVVNT
MRLWSAKAPNDFNLKDFNVGGYIQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVV
AATLQDIIRRFKSSKFGCRDPVRTNFDAFPDKVAIQLNDTHPSLAIPELMRVLVDLERLD
WDKAWEVTVKTCAYTNHTVIPEALERWPVHLLETLLPRHLQIIYEINQRFLNRVAAAFPG
DVDRLRRMSLVEEGAVKRINMAHLCIAGSHAVNGVARIHSEILKKTIFKDFYELEPHKFQ
NKTNGITPRRWLVLCNPGLAEIIAERIGEEYISDLDQLRKLLSYVDDEAFIRDVAKVKQE
NKLKFAAYLEREYKVHINPNSLFDVQVKRIHEYKRQLLNCLHVITLYNRIKKEPNKFVVP
RTVMIGGKAAPGYHMAKMIIKLITAIGDVVNHDPVVGDRLRVIFLENYRVSLAEKVIPAA
DLSEQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENFFIFGMRVEDVDR
LDQRGYNAQEYYDRIPELRQIIEQLSSGFFSPKQPDLFKDIVNMLMHHDRFKVFADYEEY
VKCQERVSALYKNPREWTRMVIRNIATSGKFSSDRTIAQYAREIWGVEPSRQRLPAPDEK
IP

Ligands and cofactors

ID	Name	Formula	Copies
PLP	Pyridoxal-5'-phosphate	C8 H10 N O6 P	1
NTF	N-(trifluoroacetyl)-beta-D-glucopyranosylamine	C8 H12 F3 N O6	1

Primary citation

Crystallographic studies on two bioisosteric analogues, N-acetyl-beta-d-glucopyranosylamine and N-trifluoroacetyl-beta-d-glucopyranosylamine, potent inhibitors of muscle glycogen phosphorylase. Anagnostou, E., Kosmopoulou, M.N., Chrysina, E.D. et al. Bioorg Med Chem (2006) 14:181-189. DOI 10.1016/j.bmc.2005.08.010 · PubMed

Other PDB entries of the same protein (UniProt P00489 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7P7D 1.45 Å, Rabbit muscle Glycogen Phosphorylase T state
2GJ4 1.6 Å, Structure of rabbit muscle glycogen phosphorylase in complex with ligand
7ONF 1.6 Å, The binding of p-coumaroyl glucose to glycogen phosphorylase reveals the relationship…
5LRF 1.75 Å, Crystal structure of Glycogen Phosphorylase b in complex with KS389
1C8K 1.76 Å, Flavopiridol inhibits glycogen phosphorylase by binding at the inhibitor site
1H5U 1.76 Å, The 1.76 a resolution crystal structure of glycogen phosphorylase B complexed with…
1A8I 1.78 Å, Spirohydantoin inhibitor of glycogen phosphorylase
5MEM 1.78 Å, A potent fluorescent inhibitor of glycogen phosphorylase as a catalytic site probe.
1K06 1.8 Å, Crystallographic Binding Study of 100 mM N-benzoyl-N'-beta-D-glucopyranosyl urea to…
2QNB 1.8 Å, Glycogen Phosphorylase b in complex with N-benzoyl-N'-beta-D-glucopyranosyl urea
2QRQ 1.8 Å, Glycogen Phosphorylase b in complex with (1R)-3'-(4-methylphenyl)-spiro[1,5-anhydro-D-glu…
4YI3 1.8 Å, Crystal structure of Gpb in complex with 4a

Browse structure collections

About this viewer

MolViewer shows 1WW3 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.