Research workbench
High resolution semet structure of the third cohesin from ruminococcus flavefaciens scaffoldin protein, scab
Analyse High resolution semet structure of the third cohesin from ruminococcus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5AOZ
- Type
- protein
- Length
- 141 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative cellulosomal scaffoldin protein
- UniProt
- A0AEF4
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative cellulosomal scaffoldin protein | protein | 141 | 0% helix, 52% strand | A0AEF4 |
Ligands and binding sites
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 3 modified (engineered).
Compared structures
- 5AOZ · High resolution SeMet structure of the third cohesin from Ruminococcus flavefaciens… · 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 A0AEF4
- Elsewhere: RCSB PDB 5AOZ · PDBe 5AOZ · UniProt A0AEF4
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