Research workbench
Crystal structure of AF1382 from archaeoglobus fulgidus, high resolution
Analyse Crystal structure of AF1382 from archaeoglobus fulgidus, high resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3OV8
- Type
- protein
- Length
- 91 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein AF_1382
- UniProt
- O28889
- Ligands
- CL
Structure
x-ray diffraction · 1 distinct chain · 64% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein AF_1382 | protein | 91 | 64% helix, 15% strand | O28889 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 3OV8 · Crystal structure of AF1382 from Archaeoglobus fulgidus, High resolution · the same entry in another collection · chain A against A, TM-score 1.00
- O28889 · AlphaFold monomer V2.0 prediction for uncharacterized protein AF_1382 (O28889) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 O28889
- Elsewhere: RCSB PDB 3OV8 · PDBe 3OV8 · UniProt O28889
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