Research workbench
Crystal structure of nfeob from P. furiosus
Analyse Crystal structure of nfeob from P. furiosus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3K53
- Type
- protein
- Length
- 1,070 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ferrous iron transport protein B
- UniProt
- Q8U2H8
- Pockets
- 7 · best druggability 0.81
Structure
x-ray diffraction · 4 distinct chains · 50% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ferrous iron transport protein B | protein | 268 | 50% helix, 17% strand | Q8U2H8 |
| B | Ferrous iron transport protein B | protein | 265 | 48% helix, 18% strand | Q8U2H8 |
| C | Ferrous iron transport protein B | protein | 267 | 49% helix, 19% strand | Q8U2H8 |
| D | Ferrous iron transport protein B | protein | 270 | 51% helix, 17% strand | Q8U2H8 |
Pockets
7 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1119 | 0.81 | 0.82 | 115 | empty |
| 2 | 526 | 0.72 | 0.81 | 67 | empty |
| 3 | 532 | 0.70 | 0.79 | 66 | empty |
| 4 | 520 | 0.70 | 0.79 | 39 | empty |
| 5 | 227 | 0.65 | 0.83 | 36 | empty |
Interfaces
3 interfaces between chains.
- C–D · 1234 Ų buried · 15 hydrogen bonds · protein-protein
- A–B · 1195 Ų buried · 12 hydrogen bonds · protein-protein
- B–D · 1039 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 3K53 · Crystal Structure of NFeoB from P. furiosus · 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 Q8U2H8
- Elsewhere: RCSB PDB 3K53 · PDBe 3K53 · UniProt Q8U2H8
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