cryo-EM structure of Cullin5 bound to RING-box protein 2 (Cul5-Rbx2). Determined by electron microscopy at 5.2 Å resolution. Released 29 Apr 2020.
Explore 6V9I in 3D Show helices and sheets RCSB PDB PDBe
6V9I contains 45 α-helices and 23 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 | 15-30 | 16 | |
| α-helix | 37-53 | 17 | |
| α-helix | 57-81 | 25 | |
| α-helix | 86-106 | 21 | |
| α-helix | 112-117 | 6 | |
| α-helix | 134-143 | 10 | |
| α-helix | 144-148 | 5 | |
| α-helix | 152-168 | 17 | |
| α-helix | 175-187 | 13 | |
| α-helix | 196-197 | 2 | |
| α-helix | 198-203 | 6 | |
| α-helix | 204-224 | 21 | |
| α-helix | 227-247 | 21 | |
| α-helix | 257-265 | 9 | |
| α-helix | 266-271 | 6 | |
| α-helix | 272-286 | 15 | |
| α-helix | 290-302 | 13 | |
| α-helix | 307-321 | 15 | |
| α-helix | 322-326 | 5 | |
| α-helix | 327-333 | 7 | |
| α-helix | 337-357 | 21 | |
| α-helix | 363-378 | 16 | |
| α-helix | 405-416 | 12 | |
| β-strand | 417 | 1 | 1 |
| α-helix | 422-424 | 3 | |
| α-helix | 427-443 | 17 | |
| α-helix | 447-464 | 18 | |
| β-strand | 467 | 1 | 1 |
| α-helix | 471-483 | 13 | |
| α-helix | 487-513 | 27 | |
| α-helix | 523-525 | 3 | |
| β-strand | 526-532 | 7 | 2 |
| α-helix | 533-536 | 4 | |
| α-helix | 546-548 | 3 | |
| α-helix | 549-552 | 4 | |
| α-helix | 555-565 | 11 | |
| β-strand | 569-572 | 4 | 2 |
| α-helix | 575-577 | 3 | |
| β-strand | 579-586 | 8 | 2 |
| β-strand | 589-596 | 8 | 2 |
| α-helix | 597-604 | 8 | |
| β-strand | 614-615 | 2 | 3 |
| α-helix | 616-623 | 8 | |
| α-helix | 627-639 | 13 | |
| β-strand | 648-650 | 3 | 3 |
| α-helix | 657-659 | 3 | |
| β-strand | 665-668 | 4 | 3 |
| β-strand | 675-676 | 2 | 4 |
| β-strand | 679-680 | 2 | 4 |
| β-strand | 683-687 | 5 | 2 |
| α-helix | 690-693 | 4 | |
| α-helix | 697-725 | 29 | |
| β-strand | 728-730 | 3 | 5 |
| α-helix | 731-742 | 12 | |
| α-helix | 750-762 | 13 | |
| β-strand | 766-769 | 4 | 5 |
| β-strand | 772-778 | 7 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 30-43 | 14 | 2 |
| β-strand | 49 | 1 | 6 |
| β-strand | 56 | 1 | 6 |
| α-helix | 64-67 | 4 | |
| β-strand | 75-78 | 4 | 7 |
| β-strand | 83-85 | 3 | 7 |
| α-helix | 86-93 | 8 | |
| β-strand | 98 | 1 | 8 |
| β-strand | 105 | 1 | 8 |
| α-helix | 106 | 1 | |
| β-strand | 108-110 | 3 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Immunoglobulin G-binding protein G,Cullin-5 | C | protein | 863 | Streptococcus sp. group G, Homo sapiens | P06654 (AlphaFold model), Q93034 (AlphaFold model) |
| RING-box protein 2 | R | protein | 113 | Mus musculus | Q9WTZ1 (AlphaFold model) |
>6V9I_1 Immunoglobulin G-binding protein G,Cullin-5 (chains C) MGSSHHHHHHSQDPMEYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGEWTYD DATKTFTVTEIPTTENLYFQGEFMATSNLLKNKGSLQFEDKWDFMRPIVLKLLRQESVTK QQWFDLFSDVHAVCLWDDKGPAKIHQALKEDILEFIKQAQARVLSHQDDTALLKAYIVEW RKFFTQCDILPKPFCQLEITLMGKQGSNKKSNVEDSIVRKLMLDTWNESIFSNIKNRLQD SAMKLVHAERLGEAFDSQLVIGVRESYVNLCSNPEDKLQIYRDNFEKAYLDSTERFYRTQ APSYLQQNGVQNYMKYADAKLKEEEKRALRYLETRRECNSVEALMECCVNALVTSFKETI LAECQGMIKRNETEKLHLMFSLMDKVPNGIEPMLKDLEEHIISAGLADMVAAAETITTDS EKYVEQLLTLFNRFSKLVKEAFQDDPRFLTARDKAYKAVVNDATIFKLELPLKQKGVGLK TQPESKCPELLANYCDMLLRKTPLSKKLTSEEIEAKLKEVLLVLKYVQNKDVFMRYHKAH LTRRLILDISADSEIEENMVEWLREVGMPADYVNKLARMFQDIKVSEDLNQAFKEMHKNN KLALPADSVNIKILNAGAWSRSSEKVFVSLPTELEDLIPEVEEFYKKNHSGRKLHWHHLM SNGIITFKNEVGQYDLEVTTFQLAVLFAWNQRPREKISFENLKLATELPDAELRRTLWSL VAFPKLKRQVLLYEPQVNSPKDFTEGTLFSVNQEFSLIKNAKVQKRGKINLIGRLQLTTE RMREEENEGIVQLRILRTQEAIIQIMKMRKKISNAQLQTELVEILKNMFLPQKKMIKEQI EWLIEHKYIRRDESDINTFIYMA
>6V9I_2 RING-box protein 2 (chains R) MADVEDGEEPCVLSSHSGSAGSKSGGDKMFSLKKWNAVAMWSWDVECDTCAICRVQVMDA CLRCQAENKQEDCVVVWGECNHSFHNCCMSLWVKQNNRCPLCQQDWVVQRIGK
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 3 |
Structure and dynamics of the ASB9 CUL-RING E3 Ligase. Lumpkin, R.J., Baker, R.W., Leschziner, A.E. et al. Nat Commun (2020) 11:2866-2866. DOI 10.1038/s41467-020-16499-9 · PubMed
Other PDB entries of the same protein (UniProt P06654 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 6V9I directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.