Research workbench
Crystal structure of an S. thermophilus nfeob T35A mutant bound to GDP
Analyse Crystal structure of an S. thermophilus nfeob T35A mutant bound to GDP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3B1Y
- Type
- protein
- Length
- 255 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ferrous iron uptake transporter protein B
- UniProt
- Q5M586
- Ligands
- GNH
- Pockets
- 1 · best druggability 0.39
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ferrous iron uptake transporter protein B | protein | 255 | 48% helix, 18% strand | Q5M586 |
Ligands and binding sites
- GNH · Aminophosphonic acid-guanylate ester · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 56 | 0.39 | 0.81 | 17 | empty |
Compared structures
- 3B1Y · Crystal structure of an S. thermophilus NFeoB T35A mutant bound to GDP · 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 Q5M586
- Elsewhere: RCSB PDB 3B1Y · PDBe 3B1Y · UniProt Q5M586
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