Structure of p97 N-D1 R155H mutant in complex with ATPgS. Determined by X-ray diffraction at 2.2 Å resolution. Released 16 Jun 2010.
Explore 3HU3 in 3D Show helices and sheets RCSB PDB PDBe
3HU3 contains 61 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 | 25-29 | 5 | 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 | 81-83 | 3 | 1 |
| α-helix | 86-91 | 6 | |
| β-strand | 99-104 | 6 | 1 |
| β-strand | 110 | 1 | 2 |
| β-strand | 113-118 | 6 | 3 |
| β-strand | 119 | 1 | 4 |
| α-helix | 120-122 | 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 |
| 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 | 306-309 | 4 | |
| β-strand | 311 | 1 | 6 |
| α-helix | 319-334 | 16 | |
| 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 | 374-384 | 11 | |
| 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 | 449-456 | 8 | |
| α-helix | 459-465 | 7 | |
| α-helix | 466-468 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 19-21 | 3 | |
| β-strand | 25-29 | 5 | 8 |
| β-strand | 38-41 | 4 | 8 |
| α-helix | 43-49 | 7 | |
| β-strand | 56-60 | 5 | 8 |
| β-strand | 66-73 | 8 | 8 |
| β-strand | 81-83 | 3 | 8 |
| α-helix | 86-91 | 6 | |
| β-strand | 99-104 | 6 | 8 |
| α-helix | 109 | 1 | |
| β-strand | 110 | 1 | 9 |
| α-helix | 111 | 1 | |
| β-strand | 113-118 | 6 | 10 |
| β-strand | 119 | 1 | 11 |
| 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 |
| β-strand | 181-183 | 3 | 10 |
| α-helix | 187-188 | 2 | |
| 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 | 306-309 | 4 | |
| 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 | 374-384 | 11 | |
| 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 | 449-458 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transitional endoplasmic reticulum ATPase | A, B | protein | 489 | Homo sapiens | P55072 (AlphaFold model) |
>3HU3_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 |
A novel ATP-dependent conformation in p97 N-D1 fragment revealed by crystal structures of disease-related mutants. Tang, W.K., Li, D., Li, C.C. et al. EMBO J (2010) 29:2217-2229. DOI 10.1038/emboj.2010.104 · 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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