Research workbench
Apostreptavidin pH 2.0 I222 complex
Analyse Apostreptavidin pH 2.0 I222 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2IZC
- Type
- protein
- Length
- 244 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Streptavidin
- UniProt
- P22629
- Ligands
- NA, CL
- Pockets
- 3 · best druggability 0.49
Structure
x-ray diffraction · 2 distinct chains · 8% helix, 57% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Streptavidin | protein | 123 | 8% helix, 58% strand | P22629 |
| D | Streptavidin | protein | 121 | 8% helix, 56% strand | P22629 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 87 | 0.49 | 0.82 | 17 | CL, NA |
| 2 | 94 | 0.47 | 0.80 | 20 | NA, CL |
| 3 | 70 | 0.32 | 0.75 | 21 | empty |
Interfaces
1 interface between chains.
- B–D · 1567 Ų buried · 28 hydrogen bonds · protein-protein
Compared structures
- 2IZC · Apostreptavidin pH 2.0 I222 complex · 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 2IZC · PDBe 2IZC · UniProt P22629
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