Research workbench
Crystal structure of neisserial surface protein a (nspa)
Analyse Crystal structure of neisserial surface protein a (nspa) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1P4T
- Type
- protein
- Length
- 155 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Outer membrane protein nspa
- UniProt
- Q9RP17
- Ligands
- CXE, ETA, SO4
- Pockets
- 3 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 77% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Outer membrane protein nspa | protein | 155 | 0% helix, 77% strand | Q9RP17 |
Ligands and binding sites
- CXE · Pentaethylene glycol monodecyl ether · ligand · 5 copies · chains A
- ETA · Ethanolamine · ligand · chains A
- SO4 · Sulfate ion · ion · chains A
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 | 58 | 0.72 | 0.99 | 21 | ETA |
| 2 | 158 | 0.52 | 0.79 | 22 | CXE |
| 3 | 75 | 0.36 | 0.77 | 18 | empty |
Compared structures
- 1P4T · Crystal structure of Neisserial surface protein A (NspA) · 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 Q9RP17
- Elsewhere: RCSB PDB 1P4T · PDBe 1P4T · UniProt Q9RP17
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