Research workbench
Streptavidin mutant S27A with biotin at 1.6A resolution
Analyse Streptavidin mutant S27A with biotin at 1.6A resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1N9M
- Type
- protein
- Length
- 488 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Streptavidin
- UniProt
- P22629
- Ligands
- BTN
- Pockets
- 6 · best druggability 0.71
Structure
x-ray diffraction · 4 distinct chains · 5% helix, 54% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Streptavidin | protein | 121 | 5% helix, 55% strand | P22629 |
| B | Streptavidin | protein | 117 | 5% helix, 57% strand | P22629 |
| C | Streptavidin | protein | 127 | 5% helix, 52% strand | P22629 |
| D | Streptavidin | protein | 123 | 5% helix, 52% strand | P22629 |
Ligands and binding sites
- BTN · Biotin · ligand · 4 copies · chains A, D, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 301 | 0.71 | 0.84 | 50 | BTN |
| 2 | 493 | 0.67 | 0.79 | 60 | empty |
| 3 | 133 | 0.64 | 0.87 | 26 | BTN |
| 4 | 148 | 0.61 | 0.84 | 28 | BTN |
| 5 | 156 | 0.55 | 0.81 | 23 | empty |
Interfaces
6 interfaces between chains.
- C–D · 1666 Ų buried · 22 hydrogen bonds · protein-protein
- A–B · 1583 Ų buried · 21 hydrogen bonds · protein-protein
- B–C · 536 Ų buried · 2 hydrogen bonds · protein-protein
- A–D · 528 Ų buried · 2 hydrogen bonds · protein-protein
- A–C · 211 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 1N9M · Streptavidin Mutant S27A with Biotin at 1.6A Resolution · 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 1N9M · PDBe 1N9M · UniProt P22629
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