6EQL: Human Glycogenin-1 (GYG1) Tyr195pIPhe mutant

Crystal Structure of Human Glycogenin-1 (GYG1) Tyr195pIPhe mutant complexed with manganese and UDP. Determined by X-ray diffraction at 2.38 Å resolution. Released 20 Dec 2017.

Method
X-ray diffraction
Resolution
2.38 Å
Organism
Homo sapiens
Chains
2
Atoms
3,843
Mol. weight
60.84 kDa
Ligands
UDP, 2PE, MN
Released
20 Dec 2017

Explore 6EQL in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6EQL contains 32 α-helices and 22 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: 18 helices, 12 β-strands

ElementResiduesLengthSheet
β-strand4-1071
α-helix13-2816
β-strand34-3961
α-helix45-5410
β-strand57-6041
α-helix71-766
α-helix78-803
α-helix81-877
α-helix88-914
β-strand97-10151
β-strand105-10732
α-helix112-1165
β-strand121-12441
α-helix1251
β-strand132-13981
α-helix143-15614
α-helix164-1707
α-helix179-1813
β-strand18211
α-helix185-1873
β-strand18912
α-helix199-2024
α-helix204-2074
β-strand210-21232
α-helix219-2213
β-strand22513
β-strand23013
α-helix244-2529
α-helix253-2575
α-helix258-2603
Chain B: 14 helices, 10 β-strands
ElementResiduesLengthSheet
β-strand4-1074
α-helix13-2816
β-strand34-3964
α-helix45-5410
β-strand57-6044
α-helix71-766
α-helix81-866
α-helix87-915
β-strand97-10154
β-strand105-10735
α-helix112-1165
β-strand121-12444
α-helix1251
β-strand132-13984
α-helix143-15614
α-helix159-1613
α-helix164-1707
α-helix179-1813
β-strand18214
α-helix185-1873
β-strand18915
β-strand210-21235
α-helix219-2213
α-helix244-25613

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Glycogenin-1A, Bprotein263Homo sapiensP46976 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>6EQL_1 Glycogenin-1 (chains A, B)
SMTDQAFVTLTTNDAYAKGALVLGSSLKQHRTTRRLVVLATPQVSDSMRKVLETVFDEVI
MVDVLDSGDSAHLTLMKRPELGVTLTKLHCWSLTQYSKCVFMDADTLVLANIDDLFDREE
LSAAPDPGWPDCFNSGVFVYQPSVETYNQLLHLASEQGSFDGGDQGILNTFFSSWATTDI
RKHLPFIYNLSSISIFSYLPAFKVFGASAKVVHFLGRVKPWNYTYDPKTKSVKSEAHDPN
MTHPEFLILWWNIFTTNVLPLLQ

Ligands and cofactors

IDNameFormulaCopies
UDPUridine-5'-diphosphateC9 H14 N2 O12 P22
2PENonaethylene glycolC18 H38 O101
MNManganese (II) ionMn2

Water and common crystallization additives (EDO) are not listed.

Primary citation

Palladium-mediated enzyme activation suggests multiphase initiation of glycogenesis. Bilyard, M.K., Bailey, H.J., Raich, L. et al. Nature (2018) 563:235-240. DOI 10.1038/s41586-018-0644-7 · PubMed

Other PDB entries of the same protein (UniProt P46976 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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