Research workbench
Streptavidin dimerized by disulfide-bonded peptide fchpqnt- NH2 dimer
Analyse Streptavidin dimerized by disulfide-bonded peptide fchpqnt- NH2 dimer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1STS
- Type
- protein
- Length
- 257 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Streptavidin; Fchpqnt-NH2
- UniProt
- P22629
- Ligands
- NH2
- Pockets
- 2 · best druggability 0.30
Structure
x-ray diffraction · 4 distinct chains · 9% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Streptavidin | protein | 123 | 11% helix, 57% strand | P22629 |
| D | Streptavidin | protein | 121 | 8% helix, 55% strand | P22629 |
| M | Fchpqnt-NH2 | protein | 6 | 0% helix, 0% strand | — |
| P | Fchpqnt-NH2 | protein | 7 | 0% helix, 0% strand | — |
Ligands and binding sites
- NH2 · Amino group · ion · 2 copies · chains M, P
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 50 | 0.30 | 0.77 | 17 | empty |
| 2 | 58 | 0.28 | 0.74 | 14 | empty |
Interfaces
3 interfaces between chains.
- B–D · 1619 Ų buried · 26 hydrogen bonds · protein-protein
- D–P · 415 Ų buried · 6 hydrogen bonds · protein-protein
- B–M · 411 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 1STS · Streptavidin dimerized by disulfide-bonded peptide fchpqnt-NH2 dimer · the same entry in another collection · chain B against B, 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 1STS · PDBe 1STS · UniProt P22629
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