Research workbench
Crystal structure of arabidopsis thaliana AGO1 mid domain in complex with cmp
Analyse Crystal structure of arabidopsis thaliana AGO1 mid domain in complex with cmp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4G0Q
- Type
- protein
- Length
- 147 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein argonaute 1
- UniProt
- O04379
- Ligands
- C5P
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein argonaute 1 | protein | 147 | 46% helix, 18% strand | O04379 |
Ligands and binding sites
- C5P · Cytidine-5'-monophosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 4G0Q · Crystal structure of Arabidopsis thaliana AGO1 MID domain in complex with CMP · the same entry in another collection · chain A against A, TM-score 1.00
- O04379 · AlphaFold monomer V2.0 prediction for protein argonaute 1 (O04379) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 O04379
- Elsewhere: RCSB PDB 4G0Q · PDBe 4G0Q · UniProt O04379
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