Research workbench
Complex crystal structure of SPE16 with ans
Analyse Complex crystal structure of SPE16 with ans in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TXC
- Type
- protein
- Length
- 314 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pathogenesis-related class 10 protein spe-16
- UniProt
- Q6T6J0
- Ligands
- 2AN
- Pockets
- 3 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Pathogenesis-related class 10 protein spe-16 | protein | 157 | 29% helix, 45% strand | Q6T6J0 |
Ligands and binding sites
- 2AN · 8-anilino-1-naphthalene sulfonate · ligand · 5 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 483 | 0.84 | 0.90 | 63 | 2AN |
| 2 | 498 | 0.84 | 0.90 | 67 | 2AN |
| 3 | 50 | 0.28 | 0.75 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 569 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 1TXC · Complex crystal structure of SPE16 with ANS · 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 Q6T6J0
- Elsewhere: RCSB PDB 1TXC · PDBe 1TXC · UniProt Q6T6J0
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