Crystal structure of the N-terminal domain of human Cul4B at 2.57A resolution. Determined by X-ray diffraction at 2.57 Å resolution. Released 29 Feb 2012.
Explore 4A64 in 3D Show helices and sheets RCSB PDB PDBe
4A64 contains 90 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 187-190 | 4 | |
| α-helix | 197-210 | 14 | |
| α-helix | 219-232 | 14 | |
| α-helix | 235-252 | 18 | |
| α-helix | 255-258 | 4 | |
| α-helix | 264-288 | 25 | |
| α-helix | 290-294 | 5 | |
| α-helix | 304-305 | 2 | |
| α-helix | 306-314 | 9 | |
| α-helix | 315-319 | 5 | |
| α-helix | 322-340 | 19 | |
| α-helix | 347-359 | 13 | |
| α-helix | 363-368 | 6 | |
| α-helix | 369-389 | 21 | |
| α-helix | 392-412 | 21 | |
| α-helix | 416-418 | 3 | |
| α-helix | 419-430 | 12 | |
| α-helix | 432-434 | 3 | |
| α-helix | 435-448 | 14 | |
| α-helix | 452-462 | 11 | |
| α-helix | 468-489 | 22 | |
| α-helix | 497-515 | 19 | |
| α-helix | 520-531 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 187-190 | 4 | |
| α-helix | 197-210 | 14 | |
| α-helix | 219-232 | 14 | |
| α-helix | 235-252 | 18 | |
| α-helix | 255-258 | 4 | |
| α-helix | 264-288 | 25 | |
| α-helix | 290-294 | 5 | |
| α-helix | 304-305 | 2 | |
| α-helix | 306-314 | 9 | |
| α-helix | 315-319 | 5 | |
| α-helix | 322-340 | 19 | |
| α-helix | 347-359 | 13 | |
| α-helix | 363-368 | 6 | |
| α-helix | 369-389 | 21 | |
| α-helix | 392-413 | 22 | |
| α-helix | 416-418 | 3 | |
| α-helix | 419-430 | 12 | |
| α-helix | 432-434 | 3 | |
| α-helix | 435-448 | 14 | |
| α-helix | 452-462 | 11 | |
| α-helix | 468-489 | 22 | |
| α-helix | 497-515 | 19 | |
| α-helix | 520-531 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 197-211 | 15 | |
| α-helix | 219-230 | 12 | |
| α-helix | 238-252 | 15 | |
| α-helix | 255-258 | 4 | |
| α-helix | 264-288 | 25 | |
| α-helix | 290-297 | 8 | |
| α-helix | 304-305 | 2 | |
| α-helix | 306-314 | 9 | |
| α-helix | 315-319 | 5 | |
| α-helix | 322-340 | 19 | |
| α-helix | 347-359 | 13 | |
| α-helix | 363-368 | 6 | |
| α-helix | 369-389 | 21 | |
| α-helix | 392-413 | 22 | |
| α-helix | 416-418 | 3 | |
| α-helix | 419-430 | 12 | |
| α-helix | 432-434 | 3 | |
| α-helix | 435-448 | 14 | |
| α-helix | 452-462 | 11 | |
| α-helix | 468-489 | 22 | |
| α-helix | 497-514 | 18 | |
| α-helix | 520-530 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 197-210 | 14 | |
| α-helix | 219-229 | 11 | |
| α-helix | 238-252 | 15 | |
| α-helix | 255-258 | 4 | |
| α-helix | 264-288 | 25 | |
| α-helix | 290-298 | 9 | |
| α-helix | 304-305 | 2 | |
| α-helix | 306-314 | 9 | |
| α-helix | 315-319 | 5 | |
| α-helix | 322-340 | 19 | |
| α-helix | 347-359 | 13 | |
| α-helix | 363-368 | 6 | |
| α-helix | 369-389 | 21 | |
| α-helix | 392-413 | 22 | |
| α-helix | 416-418 | 3 | |
| α-helix | 419-430 | 12 | |
| α-helix | 432-434 | 3 | |
| α-helix | 435-448 | 14 | |
| α-helix | 452-462 | 11 | |
| α-helix | 468-488 | 21 | |
| α-helix | 501-514 | 14 | |
| α-helix | 520-530 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cullin-4B | A, B, C, D | protein | 354 | HOMO SAPIENS | Q13620 (AlphaFold model) |
>4A64_1 CULLIN-4B (chains A, B, C, D) SMPKLPENYTDETWQKLKEAVEAIQNSTSIKYNLEELYQAVENLCSYKISANLYKQLRQI CEDHIKAQIHQFREDSLDSVLFLKKIDRCWQNHCRQMIMIRSIFLFLDRTYVLQNSMLPS IWDMGLELFRAHIISDQKVQNKTIDGILLLIERERNGEAIDRSLLRSLLSMLSDLQIYQD SFEQRFLEETNRLYAAEGQKLMQEREVPEYLHHVNKRLEEEADRLITYLDQTTQKSLIAT VEKQLLGEHLTAILQKGLNNLLDENRIQDLSLLYQLFSRVRGGVQVLLQQWIEYIKAFGS TIVINPEKDKTMRQELDDFKDKVDHIIDICFLKNEKFINAMKEAFETFINKRPN
Crystal Structure of the N-Terminal Domain of Human Cul4B at 2.57A Resolution. Vollmar, M., Ayinampudi, V., Cooper, C. et al. To be published.
Other PDB entries of the same protein (UniProt Q13620 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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