Research workbench
Structure of E. COLI nusa
Analyse Structure of E. COLI nusa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5LM9
- Type
- protein
- Length
- 319 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcription TERMINATION/ANTITERMINATION protein nusa
- UniProt
- P0AFF6
- Ligands
- MG, SO4
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcription TERMINATION/ANTITERMINATION protein nusa | protein | 319 | 46% helix, 23% strand | P0AFF6 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
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 P0AFF6
- Elsewhere: RCSB PDB 5LM9 · PDBe 5LM9 · UniProt P0AFF6
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