Research workbench
Crystal structure of a boiling stable protein SP1
Analyse Crystal structure of a boiling stable protein SP1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TR0
- Type
- protein
- Length
- 2,544 residues
- Chains
- 24
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Stable protein 1
- UniProt
- Q9AR79
- Pockets
- 20 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, R, S, T, U, V, W, X, Y | Stable protein 1 | protein | 106 | 36% helix, 30% strand | Q9AR79 |
Ligands and binding sites
- GOL · Glycerol · additive · 24 copies · chains A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, R, S, T, U, V, W, X, Y
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 579 | 0.65 | 0.76 | 95 | empty |
| 2 | 549 | 0.65 | 0.76 | 93 | empty |
| 3 | 543 | 0.62 | 0.75 | 78 | empty |
| 4 | 347 | 0.58 | 0.76 | 66 | empty |
| 5 | 88 | 0.55 | 0.85 | 15 | GOL |
Interfaces
63 interfaces between chains.
- K–L · 1672 Ų buried · 34 hydrogen bonds · protein-protein
- V–W · 1666 Ų buried · 33 hydrogen bonds · protein-protein
- C–D · 1664 Ų buried · 32 hydrogen bonds · protein-protein
- M–N · 1664 Ų buried · 34 hydrogen bonds · protein-protein
- A–B · 1663 Ų buried · 33 hydrogen bonds · protein-protein
Compared structures
- 1TR0 · Crystal Structure of a boiling stable protein SP1 · 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 Q9AR79
- Elsewhere: RCSB PDB 1TR0 · PDBe 1TR0 · UniProt Q9AR79
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