Research workbench
1.9A crystal structure of protein AQ328 from aquifex aeolicus
Analyse 1.9A crystal structure of protein AQ328 from aquifex aeolicus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1R4V
- Type
- protein
- Length
- 151 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical protein AQ_328
- UniProt
- O66665
- Ligands
- ZN
Structure
x-ray diffraction · 1 distinct chain · 62% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hypothetical protein AQ_328 | protein | 151 | 62% helix, 3% strand | O66665 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 6 modified (engineered).
Compared structures
- 1R4V · 1.9A crystal structure of protein AQ328 from Aquifex aeolicus · the same entry in another collection · chain A against A, TM-score 1.00
- O66665 · AlphaFold monomer V2.0 prediction for uncharacterized protein AQ_328 (O66665) · 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 O66665
- Elsewhere: RCSB PDB 1R4V · PDBe 1R4V · UniProt O66665
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