Human raver1 RRM1, RRM2, and RRM3 domains in complex with human vinculin tail domain Vt. Determined by X-ray diffraction at 2.75 Å resolution. Released 28 Jul 2009.
Explore 3H2U in 3D Show helices and sheets RCSB PDB PDBe
3H2U contains 38 α-helices and 44 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 | 896-910 | 15 | |
| β-strand | 912 | 1 | 1 |
| α-helix | 918-936 | 19 | |
| α-helix | 943-971 | 29 | |
| β-strand | 972 | 1 | 2 |
| α-helix | 975-986 | 12 | |
| α-helix | 988-1005 | 18 | |
| α-helix | 1013-1044 | 32 | |
| β-strand | 1048 | 1 | 2 |
| β-strand | 1060 | 1 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 41-56 | 16 | |
| β-strand | 60-64 | 5 | 3 |
| α-helix | 72-78 | 7 | |
| β-strand | 84-90 | 7 | 3 |
| β-strand | 95-100 | 6 | 3 |
| α-helix | 103-113 | 11 | |
| β-strand | 117-118 | 2 | 4 |
| β-strand | 121-122 | 2 | 4 |
| α-helix | 123 | 1 | |
| β-strand | 124-127 | 4 | 3 |
| α-helix | 128-129 | 2 | |
| β-strand | 133-137 | 5 | 5 |
| α-helix | 145-152 | 8 | |
| β-strand | 158-165 | 8 | 5 |
| β-strand | 172-180 | 9 | 5 |
| α-helix | 183-193 | 11 | |
| β-strand | 197-198 | 2 | 6 |
| β-strand | 201-202 | 2 | 6 |
| β-strand | 204-208 | 5 | 5 |
| β-strand | 222-226 | 5 | 7 |
| α-helix | 228-229 | 2 | |
| α-helix | 235-241 | 7 | |
| β-strand | 250-255 | 6 | 7 |
| β-strand | 261-268 | 8 | 7 |
| α-helix | 272-282 | 11 | |
| β-strand | 286-287 | 2 | 8 |
| β-strand | 290-291 | 2 | 8 |
| α-helix | 292 | 1 | |
| β-strand | 293-296 | 4 | 7 |
| α-helix | 297-298 | 2 | |
| α-helix | 303-315 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 896-909 | 14 | |
| β-strand | 912 | 1 | 9 |
| α-helix | 918-936 | 19 | |
| α-helix | 943-970 | 28 | |
| β-strand | 972 | 1 | 10 |
| α-helix | 975-986 | 12 | |
| α-helix | 988-1005 | 18 | |
| α-helix | 1013-1043 | 31 | |
| β-strand | 1048 | 1 | 10 |
| β-strand | 1060 | 1 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 41-56 | 16 | |
| β-strand | 60-64 | 5 | 11 |
| α-helix | 72-78 | 7 | |
| β-strand | 86-90 | 5 | 11 |
| β-strand | 95-99 | 5 | 11 |
| α-helix | 103-113 | 11 | |
| β-strand | 117-118 | 2 | 12 |
| β-strand | 121-122 | 2 | 12 |
| β-strand | 124-127 | 4 | 11 |
| α-helix | 128-129 | 2 | |
| β-strand | 133-137 | 5 | 13 |
| α-helix | 145-152 | 8 | |
| α-helix | 153-155 | 3 | |
| β-strand | 158-165 | 8 | 13 |
| β-strand | 172-180 | 9 | 13 |
| α-helix | 183-193 | 11 | |
| β-strand | 197-198 | 2 | 14 |
| β-strand | 201-202 | 2 | 14 |
| β-strand | 204-207 | 4 | 13 |
| α-helix | 215-218 | 4 | |
| β-strand | 222-226 | 5 | 15 |
| α-helix | 228-229 | 2 | |
| α-helix | 236-241 | 6 | |
| β-strand | 250-254 | 5 | 15 |
| β-strand | 262-268 | 7 | 15 |
| α-helix | 272-282 | 11 | |
| β-strand | 286-287 | 2 | 16 |
| β-strand | 290-291 | 2 | 16 |
| β-strand | 293-296 | 4 | 15 |
| α-helix | 297-298 | 2 | |
| α-helix | 303-315 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Vinculin | A, C | protein | 188 | Homo sapiens | P18206 (AlphaFold model) |
| Raver-1 | B, D | protein | 283 | Homo sapiens | Q8IY67 (AlphaFold model) |
>3H2U_1 Vinculin (chains A, C) EEKDEEFPEQKAGEVINQPMMMAARQLHDEARKWSSKGNDIIAAAKRMALLMAEMSRLVR GGSGTKRALIQCAKDIAKASDEVTRLAKEVAKQCTDKRIRTNLLQVCERIPTISTQLKIL STVKATMLGRTNISDEESEQATEMLVHNAQNLMQSVKETVREAEAASIKIRTDAGFTLRW VRKTPWYQ
>3H2U_2 Raver-1 (chains B, D) LDPEEIRKRLEHTERQFRNRRKILIRGLPGDVTNQEVHDLLSDYELKYCFVDKYKGTAFV TLLNGEQAEAAINAFHQSRLRERELSVQLQPTDALLCVANLPPSLTQQQFEELVRPFGSL ERCFLVYSERTGQSKGYGFAEYMKKDSAARAKSDLLGKPLGPRTLYVHWTDAGQLTPALL HSRCLCVDRLPPGFNDVDALCRALSAVHSPTFCQLACGQDGQLKGFAVLEYETAEMAEEA QQQADGLSLGGSHLRVSFCAPGPPGRSMLAALIAAQATALNRG
Raver1 interactions with vinculin and RNA suggest a feed-forward pathway in directing mRNA to focal adhesions. Lee, J.H., Rangarajan, E.S., Yogesha, S.D. et al. Structure (2009) 17:833-842. DOI 10.1016/j.str.2009.04.010 · PubMed
Other PDB entries of the same protein (UniProt P18206 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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