Research workbench
Cryo-EM structure of tmv with CA2+ at low pH
Analyse Cryo-EM structure of tmv with CA2+ at low pH in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6SAG
- Type
- protein + RNA
- Length
- 156 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Capsid protein; RNA (5'-R(P*GP*AP*A)-3')
- UniProt
- P69687
- Ligands
- ACE, MG, CA
Structure
electron microscopy · 2 distinct chains · 56% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Capsid protein | protein | 153 | 56% helix, 7% strand | P69687 |
| R | RNA (5'-R(P*GP*AP*A)-3') | rna | 3 | — | — |
Ligands and binding sites
- ACE · Acetyl group · ligand · chains A
- MG · Magnesium ion · metal · 4 copies · chains R
- CA · Calcium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–R · 389 Ų buried · 13 hydrogen bonds · protein-nucleic
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 6SAG · Cryo-EM structure of TMV with Ca2+ at low pH · 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 P69687
- Elsewhere: RCSB PDB 6SAG · PDBe 6SAG · UniProt P69687
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