Research workbench
T=1 capsid of an amino-terminal deletion mutant of semv cp
Analyse T=1 capsid of an amino-terminal deletion mutant of semv cp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1X36
- Type
- protein
- Length
- 198 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Coat protein
- UniProt
- Q9EB06
- Ligands
- CA
Structure
x-ray diffraction · 1 distinct chain · 22% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Coat protein | protein | 198 | 22% helix, 39% strand | Q9EB06 |
Ligands and binding sites
- CA · Calcium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1X36 · T=1 capsid of an amino-terminal deletion mutant of SeMV CP · 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 1X36 · PDBe 1X36 · UniProt Q9EB06
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