3P6Y: CF Im25-CF Im68-UGUAA complex
CF Im25-CF Im68-UGUAA complex. Determined by X-ray diffraction at 2.9 Å resolution. Released 3 Nov 2010.
- Method
- X-ray diffraction
- Resolution
- 2.9 Å
- Organism
- Homo sapiens
- Chains
- 23
- Atoms
- 17,567
- Mol. weight
- 281.11 kDa
- Released
- 3 Nov 2010
Explore 3P6Y in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
3P6Y contains 87 α-helices and 159 β-strands across 16 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.
Chain A: 8 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 36-39 | 4 | 1 |
| β-strand | 41 | 1 | 2 |
| α-helix | 42-44 | 3 | |
| β-strand | 45-50 | 6 | 3 |
| α-helix | 60-74 | 15 | |
| β-strand | 77-84 | 8 | 4 |
| β-strand | 85-88 | 4 | 2 |
| β-strand | 91-98 | 8 | 2 |
| β-strand | 104-105 | 2 | 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 |
| α-helix | 179-180 | 2 | |
| β-strand | 183-188 | 6 | 3 |
| β-strand | 192-197 | 6 | 2 |
| α-helix | 198-201 | 4 | |
| α-helix | 205-212 | 8 | |
| α-helix | 215-219 | 5 | |
| β-strand | 223-226 | 4 | 1 |
Chain B: 9 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 36-39 | 4 | 5 |
| β-strand | 41 | 1 | 6 |
| α-helix | 42-44 | 3 | |
| β-strand | 45-50 | 6 | 7 |
| α-helix | 60-73 | 14 | |
| β-strand | 77-84 | 8 | 8 |
| β-strand | 85-88 | 4 | 6 |
| β-strand | 91-99 | 9 | 6 |
| β-strand | 103-105 | 3 | 6 |
| β-strand | 108-110 | 3 | 8 |
| α-helix | 111-112 | 2 | |
| α-helix | 117-129 | 13 | |
| β-strand | 140-150 | 11 | 8 |
| β-strand | 158 | 1 | 8 |
| β-strand | 170-178 | 9 | 8 |
| β-strand | 183-188 | 6 | 7 |
| 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 |
| α-helix | 227-229 | 3 | |
Chain C: 2 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 82-86 | 5 | 9 |
| α-helix | 94-102 | 9 | |
| β-strand | 111-116 | 6 | 9 |
| β-strand | 123-130 | 8 | 9 |
| α-helix | 134-143 | 10 | |
| β-strand | 149 | 1 | 10 |
| β-strand | 152 | 1 | 10 |
| β-strand | 155-158 | 4 | 9 |
Chain D: 3 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 82-86 | 5 | 11 |
| α-helix | 94-104 | 11 | |
| β-strand | 112-116 | 5 | 11 |
| β-strand | 123-130 | 8 | 11 |
| α-helix | 134-143 | 10 | |
| α-helix | 144-146 | 3 | |
| β-strand | 149 | 1 | 12 |
| β-strand | 152 | 1 | 12 |
| β-strand | 155-158 | 4 | 11 |
Chain E: 7 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 36-39 | 4 | 13 |
| β-strand | 41 | 1 | 14 |
| α-helix | 42-44 | 3 | |
| β-strand | 45-50 | 6 | 15 |
| α-helix | 60-73 | 14 | |
| β-strand | 77-84 | 8 | 16 |
| β-strand | 85-87 | 3 | 14 |
| β-strand | 92-99 | 8 | 14 |
| β-strand | 103-105 | 3 | 14 |
| β-strand | 108-110 | 3 | 16 |
| α-helix | 111-112 | 2 | |
| α-helix | 117-128 | 12 | |
| β-strand | 140-150 | 11 | 16 |
| β-strand | 158 | 1 | 16 |
| β-strand | 170-178 | 9 | 16 |
| β-strand | 183-188 | 6 | 15 |
| β-strand | 192-197 | 6 | 14 |
| α-helix | 198-201 | 4 | |
| α-helix | 205-213 | 9 | |
| α-helix | 215-219 | 5 | |
| β-strand | 223-226 | 4 | 13 |
Chain F: 9 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 36-39 | 4 | 17 |
| β-strand | 41 | 1 | 18 |
| α-helix | 42-44 | 3 | |
| β-strand | 45-50 | 6 | 19 |
| α-helix | 60-74 | 15 | |
| β-strand | 77-84 | 8 | 20 |
| β-strand | 85-88 | 4 | 18 |
| β-strand | 91-99 | 9 | 18 |
| β-strand | 103-105 | 3 | 18 |
| β-strand | 108-110 | 3 | 20 |
| α-helix | 111-112 | 2 | |
| α-helix | 117-128 | 12 | |
| β-strand | 140-150 | 11 | 20 |
| β-strand | 158 | 1 | 20 |
| β-strand | 170-178 | 9 | 20 |
| β-strand | 183-188 | 6 | 19 |
| β-strand | 192-197 | 6 | 18 |
| 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 | 17 |
| α-helix | 227-229 | 3 | |
Chain G: 2 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 81-86 | 6 | 21 |
| α-helix | 94-104 | 11 | |
| β-strand | 109-116 | 8 | 21 |
| β-strand | 123-131 | 9 | 21 |
| α-helix | 134-142 | 9 | |
| β-strand | 149 | 1 | 22 |
| β-strand | 152 | 1 | 22 |
| β-strand | 155-157 | 3 | 21 |
Chain H: 4 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 84-86 | 3 | 23 |
| α-helix | 94-101 | 8 | |
| β-strand | 111-116 | 6 | 23 |
| β-strand | 123-130 | 8 | 23 |
| α-helix | 134-137 | 4 | |
| α-helix | 139-143 | 5 | |
| α-helix | 144-146 | 3 | |
| β-strand | 149 | 1 | 24 |
| β-strand | 152 | 1 | 24 |
| β-strand | 155-157 | 3 | 23 |
8 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Cleavage and polyadenylation specificity factor subunit 5 | A, B, E, F, I, J, M, N | protein | 202 | Homo sapiens | O43809 (AlphaFold model) |
| Cleavage and polyadenylation specificity factor subunit 6 | C, D, G, H, K, L, O, P | protein | 90 | Homo sapiens | Q16630 (AlphaFold model) |
| 5'-r(*up*gp*up*ap*a)-3' | Q, R, S, T, U, V, W | RNA | 5 | | |
Sequence of entity 1 (A, B, E, F, I, J, M, N), FASTA
>3P6Y_1 Cleavage and polyadenylation specificity factor subunit 5 (chains A, B, E, F, I, J, M, N)
ERTINLYPLTNYTFGTKEPLYEKDSSVAARFQRMREEFDKIGMRRTVEGVLIVHEHRLPH
VLLLQLGTTFFKLPGGELNPGEDEVEGLKRLMTEILGRQDGVLQDWVIDDCIGNWWRPNF
EPPQYPYIPAHITKPKEHKKLFLVQLQEKALFAVPKNYKLVAAPLFELYDNAPGYGPIIS
SLPQLLSRFNFIYNLEHHHHHH
Sequence of entity 2 (C, D, G, H, K, L, O, P), FASTA
>3P6Y_2 Cleavage and polyadenylation specificity factor subunit 6 (chains C, D, G, H, K, L, O, P)
RIALYIGNLTWWTTDEDLTEAVHSLGVNDILEIKFFENRANGQSKGFALVGVGSEASSKK
LMDLLPKRELHGQNPVVTPSNKLEHHHHHH
Sequence of entity 3 (Q, R, S, T, U, V, W), FASTA
>3P6Y_3 5'-R(*UP*GP*UP*AP*A)-3' (chains Q, R, S, T, U, V, W)
UGUAA
Primary citation
Structural basis of pre-mRNA recognition by the human cleavage factor Im complex. Li, H., Tong, S., Li, X. et al. To be published.
Other PDB entries of the same protein (UniProt O43809 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 5R4Q 1.49 Å, PanDDA analysis group deposition -- Crystal Structure of HUMAN CLEAVAGE FACTOR IM in…
- 5R4R 1.5 Å, PanDDA analysis group deposition -- Crystal Structure of HUMAN CLEAVAGE FACTOR IM in…
- 5R67 1.52 Å, PanDDA analysis group deposition -- Crystal Structure of HUMAN CLEAVAGE FACTOR IM in…
- 5R4S 1.61 Å, PanDDA analysis group deposition -- Crystal Structure of HUMAN CLEAVAGE FACTOR IM in…
- 5R4T 1.68 Å, PanDDA analysis group deposition -- Crystal Structure of HUMAN CLEAVAGE FACTOR IM in…
- 5R4P 1.78 Å, PanDDA analysis group deposition -- Crystal Structure of HUMAN CLEAVAGE FACTOR IM in…
- 3BHO 1.8 Å, Crystal Structure of the 25kDa Subunit of Human Cleavage factor Im with Ap4A
- 5R64 1.84 Å, PanDDA analysis group deposition -- Crystal Structure of HUMAN CLEAVAGE FACTOR IM in…
- 3BAP 1.85 Å, Crystal Structure of the 25 kDa Subunit of Human Cleavage Factor Im
- 2CL3 1.9 Å, Crystal structure of human Cleavage and Polyadenylation Specificity Factor 5 (CPSF5)
- 3N9U 1.92 Å, Crystal Structure of the Complex between the 25 kDa Subunit and the 59 kDa Subunit (RRM…
- 5R4U 1.92 Å, PanDDA analysis group deposition -- Crystal Structure of HUMAN CLEAVAGE FACTOR IM in…
Browse structure collections
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