Research workbench
Streptavidin in complex with nanotag
Analyse Streptavidin in complex with nanotag in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2G5L
- Type
- protein
- Length
- 240 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Streptavidin; (FME)(ASP)(VAL)(GLU)(ALA)(TRP)(LEU)
- UniProt
- P22629
- Ligands
- SO4
Structure
x-ray diffraction · 3 distinct chains · 8% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Streptavidin | protein | 121 | 7% helix, 55% strand | P22629 |
| B | Streptavidin | protein | 105 | 6% helix, 55% strand | P22629 |
| X, Y | (FME)(ASP)(VAL)(GLU)(ALA)(TRP)(LEU) | protein | 7 | 57% helix, 0% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
3 interfaces between chains.
- A–B · 1611 Ų buried · 26 hydrogen bonds · protein-protein
- A–X · 516 Ų buried · 8 hydrogen bonds · protein-protein
- B–Y · 429 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (formylation).
Compared structures
- 2G5L · Streptavidin in complex with Nanotag · 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 P22629
- Elsewhere: RCSB PDB 2G5L · PDBe 2G5L · UniProt P22629
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