1K06: Glycogen Phosphorylase

Crystallographic Binding Study of 100 mM N-benzoyl-N'-beta-D-glucopyranosyl urea to glycogen phosphorylase b. Determined by X-ray diffraction at 1.8 Å resolution. Released 3 Oct 2001.

Method
X-ray diffraction
Resolution
1.8 Å
Organism
Oryctolagus cuniculus
Chains
1
Atoms
6,909
Mol. weight
98.19 kDa
Ligands
PLP, BZD
Released
3 Oct 2001

Explore 1K06 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1K06 contains 52 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: 52 helices, 29 β-strands

ElementResiduesLengthSheet
α-helix21-3313
α-helix34-385
α-helix48-7730
α-helix79-802
β-strand81-8551
β-strand89-9242
α-helix95-1028
α-helix105-11410
α-helix119-1235
α-helix127-1282
β-strand129-13132
α-helix135-14915
β-strand154-15961
β-strand16313
α-helix1661
β-strand167-17154
β-strand174-17854
β-strand191-19221
α-helix194-1963
β-strand198-20251
β-strand205-20845
β-strand213-21645
β-strand219-231131
β-strand238-247101
α-helix262-2676
α-helix270-2734
α-helix274-2763
β-strand27813
α-helix290-31324
α-helix326-3283
α-helix329-3324
β-strand333-33861
α-helix345-3517
α-helix352-3565
α-helix361-37111
β-strand372-37541
α-helix381-3833
β-strand386-38836
α-helix389-3957
α-helix397-41721
α-helix422-4287
β-strand431-43226
β-strand438-44036
α-helix441-4477
β-strand451-45441
α-helix457-4659
α-helix469-4746
α-helix476-4783
β-strand479-48131
β-strand48617
α-helix489-4946
α-helix497-50711
α-helix510-5134
α-helix515-52410
α-helix528-55124
β-strand562-56768
α-helix576-59217
β-strand601-60668
α-helix614-63017
α-helix637-6393
β-strand640-64568
α-helix650-6567
α-helix657-6593
β-strand662-66548
α-helix667-6682
α-helix677-6837
β-strand687-69048
α-helix696-7038
α-helix705-7073
β-strand709-71028
α-helix715-72410
α-helix728-7347
α-helix736-74712
α-helix759-7679
α-helix773-79119
α-helix794-80512
α-helix809-8113
β-strand81217
α-helix813-8208
α-helix821-8255
α-helix832-8343

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Glycogen PhosphorylaseAprotein842Oryctolagus cuniculusP00489 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1K06_1 Glycogen Phosphorylase (chains A)
SRPLSDQEKRKQISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVATPRDYYFALAHTVR
DHLVGRWIRTQQHYYEKDPKRIYYLSLEFYMGRTLQNTMVNLALENACDEATYQLGLDME
ELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQKICGGWQMEEAD
DWLRYGNPWEKARPEFTLPVHFYGRVEHTSQGAKWVDTQVVLAMPYDTPVPGYRNNVVNT
MRLWSAKAPNDFNLKDFNVGGYIQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVV
AATLQDIIRRFKSSKFGCRDPVRTNFDAFPDKVAIQLNDTHPSLAIPELMRVLVDLERLD
WDKAWEVTVKTCAYTNHTVIPEALERWPVHLLETLLPRHLQIIYEINQRFLNRVAAAFPG
DVDRLRRMSLVEEGAVKRINMAHLCIAGSHAVNGVARIHSEILKKTIFKDFYELEPHKFQ
NKTNGITPRRWLVLCNPGLAEIIAERIGEEYISDLDQLRKLLSYVDDEAFIRDVAKVKQE
NKLKFAAYLEREYKVHINPNSLFDVQVKRIHEYKRQLLNCLHVITLYNRIKKEPNKFVVP
RTVMIGGKAAPGYHMAKMIIKLITAIGDVVNHDPVVGDRLRVIFLENYRVSLAEKVIPAA
DLSEQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENFFIFGMRVEDVDR
LDQRGYNAQEYYDRIPELRQIIEQLSSGFFSPKQPDLFKDIVNMLMHHDRFKVFADYEEY
VKCQERVSALYKNPREWTRMVIRNIATSGKFSSDRTIAQYAREIWGVEPSRQRLPAPDEK
IP

Ligands and cofactors

IDNameFormulaCopies
PLPPyridoxal-5'-phosphateC8 H10 N O6 P1
BZDN-[(phenylcarbonyl)carbamoyl]-beta-D-glucopyranosylamineC14 H18 N2 O72

Primary citation

Binding of N-acetyl-N '-beta-D-glucopyranosyl urea and N-benzoyl-N '-beta-D-glucopyranosyl urea to glycogen phosphorylase b: kinetic and crystallographic studies. Oikonomakos, N.G., Kosmopoulou, M., Zographos, S.E. et al. Eur J Biochem (2002) 269:1684-1696. DOI 10.1046/j.1432-1327.2002.02813.x · PubMed

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

Browse structure collections

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