6G2Y: Transitional endoplasmic reticulum ATPase

Crystal structure of the p97 D2 domain in a helical split-washer conformation. Determined by X-ray diffraction at 2.15 Å resolution. Released 10 Apr 2019.

Method
X-ray diffraction
Resolution
2.15 Å
Organism
Homo sapiens
Chains
1
Atoms
2,209
Mol. weight
35.33 kDa
Ligands
ADP, ELQ
Released
10 Apr 2019

Explore 6G2Y in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6G2Y contains 18 α-helices and 8 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: 18 helices, 8 β-strands

ElementResiduesLengthSheet
β-strand47011
α-helix476-4783
α-helix483-49816
α-helix500-5056
α-helix509-5113
β-strand513-51751
α-helix524-53411
β-strand538-54361
α-helix544-5474
α-helix558-56811
β-strand572-57761
α-helix597-60913
α-helix613-6153
β-strand617-62371
α-helix626-6283
α-helix631-6344
β-strand642-64431
α-helix646-6483
α-helix650-66011
β-strand66612
α-helix672-6776
α-helix684-70926
β-strand73112
α-helix733-7397
α-helix740-7423
α-helix749-76113

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Transitional endoplasmic reticulum ATPaseAprotein303Homo sapiensP55072 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>6G2Y_1 Transitional endoplasmic reticulum ATPase (chains A)
SALRETVVEVPQVTWEDIGGLEDVKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPG
CGKTLLAKAIANECQANFISIKGPELLTMWFGESEANVREIFDKARQAAPCVLFFDELDS
IAKARGGNIGDGGGAADRVINQILTEMDGMSTKKNVFIIGATNRPDIIDPAILRPGRLDQ
LIYIPLPDEKSRVAILKANLRKSPVAKDVDLEFLAKMTNGFSGADLTEICQRACKLAIRE
SIESEIRRERERQTNPSAMEVEEDDPVPEIRRDHFEEAMRFARRSVSDNDIRKYEMFAQT
LQQ

Ligands and cofactors

IDNameFormulaCopies
ADPAdenosine-5'-diphosphateC10 H15 N5 O10 P21
ELQ[3,4-bis(fluoranyl)phenyl]-(4-methylpiperazin-1-yl)methanoneC12 H14 F2 N2 O1

Water and common crystallization additives (MPD, DMS, NA) are not listed.

Primary citation

Crystal structure of the catalytic D2 domain of the AAA+ ATPase p97 reveals a putative helical split-washer-type mechanism for substrate unfolding. Stach, L., Morgan, R.M., Makhlouf, L. et al. FEBS Lett (2020) 594:933-943. DOI 10.1002/1873-3468.13667 · PubMed

Other PDB entries of the same protein (UniProt P55072 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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