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Structure of bacterial sylf domain containing protein, beta cell expansion factor a (befa)
Analyse Structure of bacterial sylf domain containing protein, beta cell expansion… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7RFQ
- Type
- protein
- Length
- 223 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta cell expansion factor a (befa)
- UniProt
- A0A2S3XLU2
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta cell expansion factor a (befa) | protein | 223 | 45% helix, 18% strand | A0A2S3XLU2 |
Ligands and binding sites
- CIT · Citric acid · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7RFQ · Structure of bacterial sylf domain containing protein, beta cell expansion factor a (befa) · 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 A0A2S3XLU2
- Elsewhere: RCSB PDB 7RFQ · PDBe 7RFQ · UniProt A0A2S3XLU2
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