Crystal structure of the human Fe65-PTB1 domain. Determined by X-ray diffraction at 2.2 Å resolution. Released 10 Jun 2008.
Explore 3D8D in 3D Show helices and sheets RCSB PDB PDBe
3D8D contains 9 α-helices and 14 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 |
|---|---|---|---|
| β-strand | 368-379 | 12 | 1 |
| α-helix | 382-385 | 4 | |
| α-helix | 390-401 | 12 | |
| β-strand | 421-427 | 7 | 1 |
| β-strand | 430-434 | 5 | 1 |
| β-strand | 441-446 | 6 | 1 |
| α-helix | 447-449 | 3 | |
| β-strand | 452-455 | 4 | 1 |
| β-strand | 464-470 | 7 | 1 |
| β-strand | 477-484 | 8 | 1 |
| α-helix | 488-504 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 368-379 | 12 | 2 |
| α-helix | 383-385 | 3 | |
| α-helix | 390-402 | 13 | |
| α-helix | 409-410 | 2 | |
| β-strand | 421-427 | 7 | 2 |
| β-strand | 430-434 | 5 | 2 |
| β-strand | 441-446 | 6 | 2 |
| α-helix | 447-449 | 3 | |
| β-strand | 452-455 | 4 | 2 |
| β-strand | 464-470 | 7 | 2 |
| β-strand | 477-484 | 8 | 2 |
| α-helix | 489-505 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Amyloid beta A4 precursor protein-binding family B member 1 | A, B | protein | 148 | Homo sapiens | O00213 (AlphaFold model) |
>3D8D_1 Amyloid beta A4 precursor protein-binding family B member 1 (chains A, B) GIKCFAVRSLGWVEMTEEELAPGRSSVAVNNCIRQLSYHKNNLHDPMSGGWGEGKDLLLQ LEDETLKLVEPQSQALLHAQPIISIRVWGVGRDSGRERDFAYVARDKLTQMLKCHVFRCE APAKNIATSLHEICSKIMAELEHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| HG | Mercury (II) ion | Hg | 6 |
Water and common crystallization additives (EDO) are not listed.
Crystal structure of the human Fe65-PTB1 domain. Radzimanowski, J., Ravaud, S., Schlesinger, S. et al. J Biol Chem (2008) 283:23113-23120. DOI 10.1074/jbc.M800861200 · PubMed
Other PDB entries of the same protein (UniProt O00213 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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