Research workbench
Streptavidin complexed with cyclo-ac-[chpqgppc]-NH2 monomer, pH 3.67
Analyse Streptavidin complexed with cyclo-ac-[chpqgppc]-NH2 monomer, pH 3.67 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1VWF
- Type
- protein
- Length
- 129 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Streptavidin; Peptide ligand containing hpq
- UniProt
- P22629
- Ligands
- ACE, NH2
Structure
x-ray diffraction · 2 distinct chains · 7% helix, 54% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Streptavidin | protein | 121 | 7% helix, 58% strand | P22629 |
| P | Peptide ligand containing hpq | protein | 8 | 0% helix, 0% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- B–P · 427 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 1VWF · Streptavidin complexed with cyclo-ac-[chpqgppc]-NH2 monomer, pH 3.67 · the same entry in another collection · chain P against P, 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 1VWF · PDBe 1VWF · UniProt P22629
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