Research workbench
Neisseria gonorrhoeae ferric binding protein
Analyse Neisseria gonorrhoeae ferric binding protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1D9Y
- Type
- protein
- Length
- 309 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (periplasmic iron-binding protein)
- UniProt
- Q50964
- Ligands
- FE, PO4
- Pockets
- 3 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (periplasmic iron-binding protein) | protein | 309 | 47% helix, 17% strand | Q50964 |
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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 296 | 0.65 | 0.81 | 49 | PO4 |
| 2 | 213 | 0.62 | 0.82 | 40 | empty |
| 3 | 99 | 0.44 | 0.78 | 15 | empty |
Compared structures
- 1D9Y · Neisseria gonorrhoeae ferric binding protein · 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 Q50964
- Elsewhere: RCSB PDB 1D9Y · PDBe 1D9Y · UniProt Q50964
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.