Research workbench
Primary structure of sesbania mosaic virus coat protein: its implications to the assembly and architecture of the virus
Analyse Primary structure of sesbania mosaic virus coat protein: its implications to… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SMV
- Type
- protein
- Length
- 614 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sesbania mosaic virus coat protein
- UniProt
- Q9EB06
- Ligands
- CA
- Pockets
- 1 · best druggability 0.59
Structure
x-ray diffraction · 2 distinct chains · 21% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Sesbania mosaic virus coat protein | protein | 196 | 22% helix, 40% strand | Q9EB06 |
| C | Sesbania mosaic virus coat protein | protein | 222 | 20% helix, 38% strand | Q9EB06 |
Ligands and binding sites
- CA · Calcium ion · metal · 4 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 167 | 0.59 | 0.82 | 36 | CA |
Interfaces
3 interfaces between chains.
- A–B · 945 Ų buried · 13 hydrogen bonds · protein-protein
- A–C · 932 Ų buried · 13 hydrogen bonds · protein-protein
- B–C · 926 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 1SMV · Primary structure of sesbania mosaic virus coat protein: its implications to the assembly… · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q9EB06
- Elsewhere: RCSB PDB 1SMV · PDBe 1SMV · UniProt Q9EB06
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