Structure of p97 N-D1 R155H mutant in complex with ATPgS. Determined by X-ray diffraction at 1.98 Å resolution. Released 13 Nov 2013.
Explore 4KO8 in 3D Show helices and sheets RCSB PDB PDBe
4KO8 contains 64 α-helices and 48 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 19-21 | 3 | |
| β-strand | 25-30 | 6 | 1 |
| β-strand | 38-41 | 4 | 1 |
| α-helix | 43-48 | 6 | |
| β-strand | 56-60 | 5 | 1 |
| β-strand | 66-73 | 8 | 1 |
| β-strand | 81-84 | 4 | 1 |
| α-helix | 86-92 | 7 | |
| β-strand | 99-104 | 6 | 1 |
| α-helix | 108-109 | 2 | |
| β-strand | 110 | 1 | 2 |
| α-helix | 111 | 1 | |
| β-strand | 113-118 | 6 | 3 |
| β-strand | 119 | 1 | 4 |
| α-helix | 120-122 | 3 | |
| α-helix | 130 | 1 | |
| α-helix | 131-135 | 5 | |
| α-helix | 136-139 | 4 | |
| β-strand | 144-147 | 4 | 2 |
| β-strand | 151-156 | 6 | 3 |
| β-strand | 159-169 | 11 | 3 |
| β-strand | 173-176 | 4 | 2 |
| α-helix | 180 | 1 | |
| β-strand | 181-183 | 3 | 3 |
| α-helix | 188 | 1 | |
| β-strand | 189 | 1 | 4 |
| α-helix | 190 | 1 | |
| α-helix | 191-198 | 8 | |
| α-helix | 203-205 | 3 | |
| α-helix | 210-216 | 7 | |
| α-helix | 217-221 | 5 | |
| α-helix | 222-225 | 4 | |
| α-helix | 227-233 | 7 | |
| α-helix | 236-238 | 3 | |
| β-strand | 240-244 | 5 | 5 |
| α-helix | 251-261 | 11 | |
| β-strand | 265-270 | 6 | 5 |
| α-helix | 271-275 | 5 | |
| α-helix | 278 | 1 | |
| α-helix | 281-295 | 15 | |
| β-strand | 299-304 | 6 | 5 |
| α-helix | 306-308 | 3 | |
| β-strand | 311 | 1 | 6 |
| α-helix | 319-333 | 15 | |
| β-strand | 341-347 | 7 | 5 |
| α-helix | 350-352 | 3 | |
| β-strand | 353 | 1 | 6 |
| α-helix | 355-358 | 4 | |
| β-strand | 365-368 | 4 | 5 |
| α-helix | 374-385 | 12 | |
| β-strand | 390 | 1 | 7 |
| α-helix | 396-401 | 6 | |
| α-helix | 408-424 | 17 | |
| α-helix | 439-444 | 6 | |
| β-strand | 447 | 1 | 7 |
| α-helix | 449-457 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 19-21 | 3 | |
| β-strand | 25-30 | 6 | 8 |
| β-strand | 38-41 | 4 | 8 |
| α-helix | 43-48 | 6 | |
| β-strand | 56-60 | 5 | 8 |
| β-strand | 66-73 | 8 | 8 |
| β-strand | 81-84 | 4 | 8 |
| α-helix | 86-92 | 7 | |
| β-strand | 99-104 | 6 | 8 |
| α-helix | 108-109 | 2 | |
| β-strand | 110 | 1 | 9 |
| α-helix | 111 | 1 | |
| β-strand | 113-118 | 6 | 10 |
| β-strand | 119 | 1 | 11 |
| α-helix | 120-122 | 3 | |
| α-helix | 130 | 1 | |
| α-helix | 131-135 | 5 | |
| α-helix | 136-139 | 4 | |
| β-strand | 144-147 | 4 | 9 |
| β-strand | 151-156 | 6 | 10 |
| β-strand | 159-169 | 11 | 10 |
| β-strand | 173-176 | 4 | 9 |
| α-helix | 180 | 1 | |
| β-strand | 181-183 | 3 | 10 |
| α-helix | 188 | 1 | |
| β-strand | 189 | 1 | 11 |
| α-helix | 190 | 1 | |
| α-helix | 191-198 | 8 | |
| α-helix | 203-205 | 3 | |
| α-helix | 210-216 | 7 | |
| α-helix | 217-221 | 5 | |
| α-helix | 222-225 | 4 | |
| α-helix | 227-233 | 7 | |
| α-helix | 236-238 | 3 | |
| β-strand | 240-244 | 5 | 12 |
| α-helix | 251-261 | 11 | |
| β-strand | 265-270 | 6 | 12 |
| α-helix | 271-275 | 5 | |
| α-helix | 278 | 1 | |
| α-helix | 281-295 | 15 | |
| β-strand | 299-304 | 6 | 12 |
| α-helix | 306-308 | 3 | |
| β-strand | 311 | 1 | 13 |
| α-helix | 319-334 | 16 | |
| β-strand | 341-347 | 7 | 12 |
| α-helix | 350-352 | 3 | |
| β-strand | 353 | 1 | 13 |
| α-helix | 355-358 | 4 | |
| β-strand | 365-368 | 4 | 12 |
| α-helix | 374-385 | 12 | |
| β-strand | 390 | 1 | 14 |
| α-helix | 396-401 | 6 | |
| α-helix | 408-424 | 17 | |
| α-helix | 439-444 | 6 | |
| β-strand | 447 | 1 | 14 |
| α-helix | 449-457 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transitional endoplasmic reticulum ATPase | A, B | protein | 489 | Homo sapiens | P55072 (AlphaFold model) |
>4KO8_1 Transitional endoplasmic reticulum ATPase (chains A, B) MASGADSKGDDLSTAILKQKNRPNRLIVDEAINEDNSVVSLSQPKMDELQLFRGDTVLLK GKKRREAVCIVLSDDTCSDEKIRMNRVVRNNLRVRLGDVISIQPCPDVKYGKRIHVLPID DTVEGITGNLFEVYLKPYFLEAYRPIRKGDIFLVHGGMRAVEFKVVETDPSPYCIVAPDT VIHCEGEPIKREDEEESLNEVGYDDIGGCRKQLAQIKEMVELPLRHPALFKAIGVKPPRG ILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESESNLRKAFEEAEKNAPAI IFIDELDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRF GRFDREVDIGIPDATGRLEILQIHTKNMKLADDVDLEQVANETHGHVGADLAALCSEAAL QAIRKKMDLIDLEDETIDAEVMNSLAVTMDDFRWALSQSNPSALRETVVEVPQVTWEDIG GRSHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| MG | Magnesium ion | Mg | 2 |
| AGS | Phosphothiophosphoric acid-adenylate ester | C10 H16 N5 O12 P3 S | 2 |
Altered Intersubunit Communication Is the Molecular Basis for Functional Defects of Pathogenic p97 Mutants. Tang, W.K., Xia, D. J Biol Chem (2013) 288:36624-36635. DOI 10.1074/jbc.M113.488924 · PubMed
Other PDB entries of the same protein (UniProt P55072 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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