3EBB: PLAP/P97 complex

PLAP/P97 complex. Determined by X-ray diffraction at 1.9 Å resolution. Released 24 Feb 2009.

Method
X-ray diffraction
Resolution
1.9 Å
Organisms
HOMO SAPIENS, Homo sapiens
Chains
8
Atoms
8,729
Mol. weight
139.39 kDa
Ligands
MG
Released
24 Feb 2009

Explore 3EBB in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3EBB contains 77 α-helices and 0 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: 20 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix548-55912
α-helix564-5663
α-helix567-5693
α-helix570-58415
α-helix590-5923
α-helix593-60311
α-helix611-62010
α-helix624-6318
α-helix636-64510
α-helix653-66614
α-helix670-6789
α-helix680-6889
α-helix689-6913
α-helix696-71520
α-helix719-73315
α-helix739-75315
α-helix757-7659
α-helix768-7714
α-helix772-7776
α-helix782-79211
Chain B: 19 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix548-55912
α-helix567-5693
α-helix570-58415
α-helix590-5923
α-helix593-60311
α-helix607-6093
α-helix611-62010
α-helix624-6318
α-helix636-64510
α-helix653-66614
α-helix670-6789
α-helix680-68910
α-helix696-71520
α-helix722-73514
α-helix739-75315
α-helix757-76610
α-helix768-7725
α-helix773-7764
α-helix782-79413
Chain C: 20 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix548-55912
α-helix567-5693
α-helix570-58415
α-helix590-5923
α-helix593-60210
α-helix607-6093
α-helix611-62010
α-helix624-6318
α-helix636-64712
α-helix653-66614
α-helix670-6789
α-helix680-6878
α-helix688-6914
α-helix696-71621
α-helix719-73315
α-helix739-75315
α-helix757-7659
α-helix768-7725
α-helix773-7775
α-helix782-79413
Chain D: 18 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix548-55912
α-helix567-5693
α-helix570-58516
α-helix590-5923
α-helix593-60210
α-helix611-62010
α-helix624-6318
α-helix636-64510
α-helix653-66614
α-helix670-6789
α-helix680-68910
α-helix696-71520
α-helix722-73514
α-helix739-75315
α-helix757-76610
α-helix768-7725
α-helix773-7775
α-helix782-79413

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Phospholipase A2-activating proteinA, B, C, Dprotein304HOMO SAPIENSQ9Y263 (AlphaFold model)
Transitional endoplasmic reticulum atpase (ter ATPE, F, G, Hprotein10Homo sapiensP55072 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>3EBB_1 PHOSPHOLIPASE A2-ACTIVATING PROTEIN (chains A, B, C, D)
MGSSHHHHHHSSGLVPRGSMAGVDPFTGNSAYRSAASKTMNIYFPKKEAVTFDQANPTQI
LGKLKELNGTAPEEKKLTEDDLILLEKILSLICNSSSEKPTVQQLQILWKAINCPEDIVF
PALDILRLSIKHPSVNENFCNEKEGAQFSSHLINLLNPKGKPANQLLALRTFCNCFVGQA
GQKLMMSQRESLMSHAIELKSGSNKNIHIALATLALNYSVCFHKDHNIEGKAQCLSLIST
ILEVVQDLEATFRLLVALGTLISDDSNAVQLAKSLGVDSQIKKYSSVSEPAKVSECCRFI
LNLL
Sequence of entity 2 (E, F, G, H), FASTA
>3EBB_2 TRANSITIONAL ENDOPLASMIC RETICULUM ATPASE (TER ATP (chains E, F, G, H)
TEDNDDDLYG

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg1

Primary citation

Structure and function of the PLAA/Ufd3-p97/Cdc48 complex. Qiu, L., Pashkova, N., Walker, J.R. et al. J Biol Chem (2010) 285:365-372. DOI 10.1074/jbc.M109.044685 · PubMed

Other PDB entries of the same protein (UniProt Q9Y263 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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