2WOJ: ADP-AlF4 complex of S. cerevisiae GET3

ADP-AlF4 complex of S. cerevisiae GET3. Determined by X-ray diffraction at 1.99 Å resolution. Released 11 Aug 2009.

Method
X-ray diffraction
Resolution
1.99 Å
Organism
SACCHAROMYCES CEREVISIAE
Chains
4
Atoms
10,014
Mol. weight
159.92 kDa
Ligands
ZN, MG, ALF, ADP
Released
11 Aug 2009

Explore 2WOJ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2WOJ contains 66 α-helices and 32 β-strands across 4 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: 17 helices, 8 β-strands

ElementResiduesLengthSheet
α-helix10-134
β-strand20-2561
α-helix31-4515
β-strand51-5551
α-helix62-665
β-strand75-7621
α-helix771
β-strand83-8751
α-helix90-989
α-helix125-1306
α-helix136-15419
β-strand162-16651
α-helix167-1693
α-helix170-1778
α-helix179-18810
α-helix213-23018
β-strand236-24381
α-helix246-26116
β-strand266-27491
α-helix286-30520
β-strand310-31561
α-helix316-3172
α-helix323-33513
α-helix340-3434
α-helix344-3507
Chain B: 16 helices, 8 β-strands
ElementResiduesLengthSheet
α-helix10-134
β-strand20-2562
α-helix31-4515
β-strand51-5552
α-helix62-665
β-strand75-7622
α-helix771
β-strand83-8752
α-helix90-10314
α-helix127-1304
α-helix136-15217
β-strand162-16652
α-helix167-1693
α-helix170-18920
α-helix212-23019
β-strand236-24382
α-helix246-26116
β-strand266-27492
α-helix286-30520
β-strand310-31562
α-helix316-3172
α-helix324-33512
α-helix340-3434
α-helix344-3485
Chain C: 16 helices, 8 β-strands
ElementResiduesLengthSheet
α-helix10-134
β-strand20-2563
α-helix31-4515
β-strand51-5553
α-helix62-665
β-strand75-7623
α-helix771
β-strand83-8753
α-helix90-978
α-helix127-1304
α-helix136-15015
β-strand162-16653
α-helix167-1693
α-helix170-18718
α-helix214-23017
β-strand236-24383
α-helix246-26116
β-strand266-27493
α-helix286-30520
β-strand310-31563
α-helix316-3172
α-helix323-33513
α-helix340-3434
α-helix346-3494
Chain D: 17 helices, 8 β-strands
ElementResiduesLengthSheet
α-helix10-134
β-strand20-2454
α-helix31-4515
β-strand51-5554
α-helix62-665
β-strand75-7624
α-helix771
β-strand83-8754
α-helix90-10314
α-helix119-1224
α-helix126-1305
α-helix136-15015
β-strand162-16654
α-helix167-1693
α-helix170-18819
α-helix213-23018
β-strand236-24384
α-helix246-26116
β-strand268-27474
α-helix286-30520
β-strand310-31564
α-helix316-3172
α-helix324-33512
α-helix340-3434
α-helix344-3485

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Atpase GET3A, B, C, Dprotein354SACCHAROMYCES CEREVISIAEQ12154 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>2WOJ_1 ATPASE GET3 (chains A, B, C, D)
MDLTVEPNLHSLITSTTHKWIFVGGKGGVGKTTSSCSIAIQMALSQPNKQFLLISTDPAH
NLSDAFGEKFGKDARKVTGMNNLSCMEIDPSAALKDMNDMAVSRANNNGSDGQGDDLGSL
LQGGALADLTGSIPGIDEALSFMEVMKHIKRQEQGEGETFDTVIFDTAPTGHTLRFLQLP
NTLSKLLEKFGEITNKLGPMLNSFMGAGNVDISGKLNELKANVETIRQQFTDPDLTTFVC
VCISEFLSLYETERLIQELISYDMDVNSIIVNQLLFAENDQEHNCKRCQARWKMQKKYLD
QIDELYEDFHVVKMPLCAGEIRGLNNLTKFSQFLNKEYNPITDGKVIYELEDKE

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn2
MGMagnesium ionMg4
ALFTetrafluoroaluminate ionAl F44
ADPAdenosine-5'-diphosphateC10 H15 N5 O10 P24

Primary citation

The Structural Basis of Tail-Anchored Membrane Protein Recognition by Get3. Mateja, A., Szlachcic, A., Downing, M.E. et al. Nature (2009) 461:361. DOI 10.1038/NATURE08319 · PubMed

Other PDB entries of the same protein (UniProt Q12154 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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