4GQH: Capsid protein
The Conformations and Interactions of the Four-Layer Aggregate Revealed by X-ray Crystallography Diffraction Implied the Importance of Peptides at Opposite Ends in Their Assemblies. Determined by X-ray diffraction at 3.06 Å resolution. Released 28 Aug 2013.
- Method
- X-ray diffraction
- Resolution
- 3.06 Å
- Organism
- Tobacco mosaic virus
- Chains
- 34
- Atoms
- 36,918
- Mol. weight
- 657.92 kDa
- Released
- 28 Aug 2013
Explore 4GQH in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
4GQH contains 234 α-helices and 264 β-strands across 34 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: 6 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 1-3 | 3 | 4 |
| α-helix | 7-13 | 7 | |
| β-strand | 17-18 | 2 | 5 |
| α-helix | 20-30 | 11 | |
| α-helix | 38-50 | 13 | |
| β-strand | 53 | 1 | 5 |
| β-strand | 57 | 1 | 6 |
| β-strand | 60 | 1 | 6 |
| β-strand | 67-70 | 4 | 5 |
| α-helix | 77-86 | 10 | |
| α-helix | 116-134 | 19 | |
| β-strand | 138-140 | 3 | 5 |
| α-helix | 141-148 | 8 | |
| β-strand | 151-153 | 3 | 4 |
Chain A: 7 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 1-3 | 3 | 1 |
| α-helix | 4 | 1 | |
| α-helix | 9-12 | 4 | |
| β-strand | 17-18 | 2 | 2 |
| α-helix | 20-30 | 11 | |
| α-helix | 38-50 | 13 | |
| β-strand | 53 | 1 | 2 |
| β-strand | 57 | 1 | 3 |
| β-strand | 60 | 1 | 3 |
| β-strand | 68-70 | 3 | 2 |
| α-helix | 76-86 | 11 | |
| α-helix | 110-134 | 25 | |
| β-strand | 138-139 | 2 | 2 |
| α-helix | 141-148 | 8 | |
| β-strand | 151-153 | 3 | 1 |
Chain b: 6 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-3 | 2 | 9 |
| α-helix | 7-11 | 5 | |
| β-strand | 17-18 | 2 | 10 |
| α-helix | 20-30 | 11 | |
| α-helix | 38-50 | 13 | |
| β-strand | 53 | 1 | 10 |
| β-strand | 68-70 | 3 | 10 |
| α-helix | 76-86 | 11 | |
| α-helix | 115-133 | 19 | |
| β-strand | 138-139 | 2 | 10 |
| α-helix | 141-148 | 8 | |
| β-strand | 151-152 | 2 | 9 |
Chain B: 7 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 1-3 | 3 | 7 |
| α-helix | 4 | 1 | |
| α-helix | 7-13 | 7 | |
| β-strand | 17-18 | 2 | 8 |
| α-helix | 20-30 | 11 | |
| α-helix | 38-50 | 13 | |
| β-strand | 53 | 1 | 8 |
| β-strand | 68-70 | 3 | 8 |
| α-helix | 77-86 | 10 | |
| α-helix | 110-134 | 25 | |
| β-strand | 138-139 | 2 | 8 |
| α-helix | 141-147 | 7 | |
| β-strand | 151-153 | 3 | 7 |
Chain c: 8 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 1-3 | 3 | 14 |
| α-helix | 7-10 | 4 | |
| β-strand | 17-18 | 2 | 15 |
| α-helix | 20-30 | 11 | |
| α-helix | 38-50 | 13 | |
| β-strand | 53 | 1 | 15 |
| β-strand | 57 | 1 | 16 |
| β-strand | 60 | 1 | 16 |
| α-helix | 61 | 1 | |
| α-helix | 63 | 1 | |
| β-strand | 67-70 | 4 | 15 |
| α-helix | 76-86 | 11 | |
| α-helix | 117-133 | 17 | |
| β-strand | 138-140 | 3 | 15 |
| α-helix | 141-148 | 8 | |
| β-strand | 151-153 | 3 | 14 |
Chain C: 6 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2 | 1 | 11 |
| α-helix | 7-13 | 7 | |
| β-strand | 17-18 | 2 | 12 |
| α-helix | 20-30 | 11 | |
| α-helix | 38-50 | 13 | |
| β-strand | 53 | 1 | 12 |
| β-strand | 57 | 1 | 13 |
| β-strand | 60 | 1 | 13 |
| β-strand | 68-70 | 3 | 12 |
| α-helix | 76-86 | 11 | |
| α-helix | 112-133 | 22 | |
| β-strand | 138-139 | 2 | 12 |
| α-helix | 141-148 | 8 | |
| β-strand | 152 | 1 | 11 |
Chain d: 7 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 1-3 | 3 | 20 |
| α-helix | 4 | 1 | |
| α-helix | 7-13 | 7 | |
| β-strand | 17-18 | 2 | 21 |
| α-helix | 20-30 | 11 | |
| α-helix | 38-50 | 13 | |
| β-strand | 53 | 1 | 21 |
| β-strand | 57 | 1 | 22 |
| β-strand | 60 | 1 | 22 |
| β-strand | 68-70 | 3 | 21 |
| α-helix | 76-86 | 11 | |
| α-helix | 115-134 | 20 | |
| β-strand | 138-139 | 2 | 21 |
| α-helix | 141-148 | 8 | |
| β-strand | 151-153 | 3 | 20 |
Chain D: 9 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-3 | 2 | 17 |
| α-helix | 4 | 1 | |
| α-helix | 9-12 | 4 | |
| β-strand | 17-18 | 2 | 18 |
| α-helix | 20-30 | 11 | |
| α-helix | 38-50 | 13 | |
| β-strand | 53 | 1 | 18 |
| β-strand | 57 | 1 | 19 |
| β-strand | 60 | 1 | 19 |
| α-helix | 61-63 | 3 | |
| β-strand | 68-70 | 3 | 18 |
| α-helix | 76-86 | 11 | |
| α-helix | 108-112 | 5 | |
| α-helix | 115-134 | 20 | |
| β-strand | 138-139 | 2 | 18 |
| α-helix | 141-148 | 8 | |
| β-strand | 151-152 | 2 | 17 |
26 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 |
|---|
| Capsid protein | A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X, Y, Z, a, b, c, d, e, f, h, i | protein | 174 | Tobacco mosaic virus | P69687 |
Sequence of entity 1 (A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X, Y, Z, a, b, c, d, e, f, h, i), FASTA
>4GQH_1 Capsid protein (chains A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X, Y, Z, a, b, c, d, e, f, h, i)
MGSSHHHHHHSSGLVPRGSHSYSITTPSQFVFLSSAWADPIELINLCTNALGNQFQTQQA
RTVVQRQFSEVWKPSPQVTVRFPDSDFKVYRYNAVLDPLVTALLGAFDTRNRIIEVENQA
NPTTAETLDATRRVDDATVAIRSAINNLIVELIRGTGSYNRSSFESSSGLVWTS
Primary citation
The Conformations and Interactions of the Four-Layer Aggregate Revealed by X-ray Crystallography Diffraction Implied the Importance of Peptides at Opposite Ends in Their Assemblies. Li, X.Y., Song, B.A., Hu, D.Y. et al. To be published.
Other PDB entries of the same protein (UniProt P69687), best resolution first:
- 6SAE 1.9 Å, Cryo-EM structure of TMV in water
- 6R7M 1.92 Å, Tobacco Mosaic Virus (TMV)
- 6SAG 2.0 Å, Cryo-EM structure of TMV with Ca2+ at low pH
- 6I5A 2.3 Å, Tobacco Mosaic Virus
- 6RLP 2.3 Å, Cryo-EM reconstruction of TMV coat protein
- 1EI7 2.45 Å, Tmv coat protein refined from the 4-layer aggregate
- 8EAW 2.8 Å, An asymmetric disk assembly formed by tandem dimers of the tobacco mosaic viral capsid…
- 2TMV 2.9 Å, Visualization of protein-nucleic acid interactions in a virus. Refined structure of…
- 6X0Q 3.0 Å, A Circular Permutant of the Tobacco Mosaic Virus (TMV) mutant Q101H coordinated with heme
- 6X0R 3.0 Å, A Circular Permutant of the Tobacco Mosaic Virus (TMV) mutant Q101H
- 3KML 3.01 Å, Circular Permutant of the Tobacco Mosaic Virus
- 3J06 3.3 Å, CryoEM Helical Reconstruction of TMV
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