Crystal Structure of CFIm68 RRM/CFIm25 complex. Determined by X-ray diffraction at 2.9 Å resolution. Released 16 Feb 2011.
Explore 3Q2S in 3D Show helices and sheets RCSB PDB PDBe
3Q2S contains 27 α-helices and 42 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 | 23-25 | 3 | |
| α-helix | 27-30 | 4 | |
| β-strand | 35-39 | 5 | 1 |
| β-strand | 41 | 1 | 2 |
| α-helix | 42-44 | 3 | |
| β-strand | 45-50 | 6 | 3 |
| α-helix | 60-73 | 14 | |
| β-strand | 77-84 | 8 | 4 |
| β-strand | 85-87 | 3 | 2 |
| β-strand | 92-99 | 8 | 2 |
| β-strand | 103-105 | 3 | 2 |
| β-strand | 108-110 | 3 | 4 |
| α-helix | 111-112 | 2 | |
| α-helix | 117-129 | 13 | |
| β-strand | 140-150 | 11 | 4 |
| β-strand | 158 | 1 | 4 |
| β-strand | 170-178 | 9 | 4 |
| β-strand | 183-188 | 6 | 3 |
| β-strand | 192-197 | 6 | 2 |
| α-helix | 198-201 | 4 | |
| α-helix | 205-208 | 4 | |
| α-helix | 212-214 | 3 | |
| α-helix | 215-219 | 5 | |
| β-strand | 222-226 | 5 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 22-25 | 4 | |
| α-helix | 27-30 | 4 | |
| β-strand | 36-39 | 4 | 5 |
| β-strand | 41 | 1 | 6 |
| α-helix | 42-44 | 3 | |
| β-strand | 45-47 | 3 | 7 |
| β-strand | 50 | 1 | 8 |
| α-helix | 51-53 | 3 | |
| α-helix | 62-73 | 12 | |
| β-strand | 77-83 | 7 | 9 |
| β-strand | 85-88 | 4 | 6 |
| β-strand | 91-98 | 8 | 6 |
| β-strand | 104-105 | 2 | 6 |
| β-strand | 108-110 | 3 | 9 |
| α-helix | 111-112 | 2 | |
| α-helix | 117-128 | 12 | |
| β-strand | 140-150 | 11 | 9 |
| β-strand | 158 | 1 | 9 |
| β-strand | 170-178 | 9 | 9 |
| β-strand | 183-185 | 3 | 7 |
| β-strand | 188 | 1 | 8 |
| β-strand | 192-197 | 6 | 6 |
| α-helix | 198-201 | 4 | |
| α-helix | 205-208 | 4 | |
| α-helix | 212-214 | 3 | |
| α-helix | 215-219 | 5 | |
| β-strand | 223-226 | 4 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 82-86 | 5 | 10 |
| α-helix | 94-102 | 9 | |
| β-strand | 109-116 | 8 | 10 |
| β-strand | 123-131 | 9 | 10 |
| α-helix | 136-141 | 6 | |
| β-strand | 149 | 1 | 11 |
| β-strand | 152 | 1 | 11 |
| β-strand | 155-158 | 4 | 10 |
| α-helix | 161-170 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 82 | 1 | 12 |
| β-strand | 83-84 | 2 | 13 |
| β-strand | 85-86 | 2 | 12 |
| α-helix | 95-104 | 10 | |
| β-strand | 109-116 | 8 | 12 |
| β-strand | 123-131 | 9 | 12 |
| α-helix | 137-142 | 6 | |
| β-strand | 157-158 | 2 | 13 |
| α-helix | 161-168 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cleavage and polyadenylation specificity factor subunit 5 | A, B | protein | 207 | Homo sapiens | O43809 (AlphaFold model) |
| Cleavage and polyadenylation specificity factor subunit 6 | C, D | protein | 229 | Homo sapiens | Q16630 (AlphaFold model) |
>3Q2S_1 Cleavage and polyadenylation specificity factor subunit 5 (chains A, B) GNKYIQQTKPLTLERTINLYPLTNYTFGTKEPLYEKDSSVAARFQRMREEFDKIGMRRTV EGVLIVHEHRLPHVLLLQLGTTFFKLPGGELNPGEDEVEGLKRLMTEILGRQDGVLQDWV IDDCIGNWWRPNFEPPQYPYIPAHITKPKEHKKLFLVQLQEKALFAVPKNYKLVAAPLFE LYDNAPGYGPIISSLPQLLSRFNFIYN
>3Q2S_2 Cleavage and polyadenylation specificity factor subunit 6 (chains C, D) DVGEEFNQEAEYGGHDQIDLYDDVISPSANNGDAPEDRDYMDTLPPTVGDDVGKGAAPNV VYTYTGKRIALYIGNLTWWTTDEDLTEAVHSLGVNDILEIKFFENRANGQSKGFALVGVG SEASSKKLMDLLPKRELHGQNPVVTPVNKQFLSQFEMQSRKTTQSGQMSGEGKAGPPGGS SRAAFPQGGRGRGRFPGAVPGGDRFPGPAGPGGPPPPFPAGQTHHHHHH
Crystal Structure of a Human Cleavage Factor CFI(m)25/CFI(m)68/RNA Complex Provides an Insight into Poly(A) Site Recognition and RNA Looping. Yang, Q., Coseno, M., Gilmartin, G.M. et al. Structure (2011) 19:368-377. DOI 10.1016/j.str.2010.12.021 · PubMed
Other PDB entries of the same protein (UniProt O43809 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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