Structure of p97 N-D1 L198W mutant in complex with ADP. Determined by X-ray diffraction at 2.2 Å resolution. Released 10 Feb 2016.
Explore 5DYG in 3D Show helices and sheets RCSB PDB PDBe
5DYG contains 27 α-helices and 24 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 25-30 | 6 | 1 |
| β-strand | 38-41 | 4 | 1 |
| α-helix | 43-49 | 7 | |
| 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 |
| β-strand | 110 | 1 | 2 |
| β-strand | 113-118 | 6 | 3 |
| β-strand | 119 | 1 | 4 |
| α-helix | 120-123 | 4 | |
| 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 |
| β-strand | 181-183 | 3 | 3 |
| α-helix | 187-188 | 2 | |
| β-strand | 189 | 1 | 4 |
| α-helix | 190 | 1 | |
| α-helix | 191-193 | 3 | |
| α-helix | 203-205 | 3 | |
| α-helix | 210-225 | 16 | |
| α-helix | 229-232 | 4 | |
| α-helix | 235-238 | 4 | |
| β-strand | 240-244 | 5 | 5 |
| α-helix | 251-262 | 12 | |
| 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 | |
| α-helix | 335-337 | 3 | |
| β-strand | 341-347 | 7 | 5 |
| β-strand | 353 | 1 | 6 |
| α-helix | 355-358 | 4 | |
| β-strand | 365-368 | 4 | 5 |
| α-helix | 374-385 | 12 | |
| β-strand | 389-390 | 2 | 7 |
| α-helix | 396-402 | 7 | |
| α-helix | 408-432 | 25 | |
| α-helix | 435-437 | 3 | |
| α-helix | 439-444 | 6 | |
| β-strand | 446-447 | 2 | 7 |
| α-helix | 449-456 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transitional endoplasmic reticulum ATPase | A | protein | 468 | Homo sapiens | P55072 (AlphaFold model) |
>5DYG_1 Transitional endoplasmic reticulum ATPase (chains A) MASGADSKGDDLSTAILKQKNRPNRLIVDEAINEDNSVVSLSQPKMDELQLFRGDTVLLK GKKRREAVCIVLSDDTCSDEKIRMNRVVRNNLRVRLGDVISIQPCPDVKYGKRIHVLPID DTVEGITGNLFEVYLKPYFLEAYRPIRKGDIFLVRGGMRAVEFKVVETDPSPYCIVAPDT VIHCEGEPIKREDEEESWNEVGYDDIGGCRKQLAQIKEMVELPLRHPALFKAIGVKPPRG ILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESESNLRKAFEEAEKNAPAI IFIDELDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRF GRFDREVDIGIPDATGRLEILQIHTKNMKLADDVDLEQVANETHGHVGADLAALCSEAAL QAIRKKMDLIDLEDETIDAEVMNSLAVTMDDFRWALSQSNRSHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 1 |
Role of the D1-D2 Linker of Human VCP/p97 in the Asymmetry and ATPase Activity of the D1-domain. Tang, W.K., Xia, D. Sci Rep (2016) 6:20037-20037. DOI 10.1038/srep20037 · 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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