Research workbench
Streptavidin dimerized by disulfide-bonded peptide ac- chpqnt-NH2 dimer
Analyse Streptavidin dimerized by disulfide-bonded peptide ac- chpqnt-NH2 dimer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1STR
- Type
- protein
- Length
- 256 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Streptavidin; Ac-chpqnt-NH2
- UniProt
- P22629
- Ligands
- ACE, NH2
- Pockets
- 1 · best druggability 0.36
Structure
x-ray diffraction · 3 distinct chains · 8% helix, 55% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Streptavidin | protein | 123 | 8% helix, 57% strand | P22629 |
| D | Streptavidin | protein | 121 | 8% helix, 56% strand | P22629 |
| M, P | Ac-chpqnt-NH2 | protein | 6 | 0% helix, 0% strand | — |
Ligands and binding sites
- ACE · Acetyl group · ligand · 2 copies · chains M, P
- 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
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 95 | 0.36 | 0.76 | 29 | empty |
Interfaces
3 interfaces between chains.
- B–D · 1610 Ų buried · 23 hydrogen bonds · protein-protein
- B–M · 404 Ų buried · 4 hydrogen bonds · protein-protein
- D–P · 388 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent (covalent ligand).
Compared structures
- 1STR · Streptavidin dimerized by disulfide-bonded peptide ac-chpqnt-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 1STR · PDBe 1STR · UniProt P22629
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