Research workbench
X-ray crystal structure of protein FN1578 from fusobacterium nucleatum. northeast structural genomics consortium target NR1.
Analyse X-ray crystal structure of protein FN1578 from fusobacterium nucleatum.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2GSL
- Type
- protein
- Length
- 734 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical protein
- Ligands
- MG
- Pockets
- 12 · best druggability 0.75
Structure
x-ray diffraction · 6 distinct chains · 70% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hypothetical protein | protein | 124 | 72% helix, 1% strand | — |
| B | Hypothetical protein | protein | 119 | 69% helix, 0% strand | — |
| C | Hypothetical protein | protein | 122 | 74% helix, 1% strand | — |
| D | Hypothetical protein | protein | 121 | 66% helix, 0% strand | — |
| E | Hypothetical protein | protein | 121 | 67% helix, 0% strand | — |
| F | Hypothetical protein | protein | 127 | 73% helix, 0% strand | — |
Ligands and binding sites
- MG · Magnesium ion · metal · 6 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 982 | 0.75 | 0.78 | 88 | empty |
| 2 | 167 | 0.50 | 0.77 | 25 | empty |
| 3 | 177 | 0.46 | 0.75 | 21 | MG |
| 4 | 91 | 0.45 | 0.79 | 18 | empty |
| 5 | 143 | 0.45 | 0.76 | 19 | MG |
Interfaces
9 interfaces between chains.
- C–D · 1133 Ų buried · 6 hydrogen bonds · protein-protein
- A–B · 1088 Ų buried · 9 hydrogen bonds · protein-protein
- E–F · 1055 Ų buried · 7 hydrogen bonds · protein-protein
- C–F · 374 Ų buried · 5 hydrogen bonds · protein-protein
- A–C · 218 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 modified (engineered).
Compared structures
- 2GSL · X-Ray Crystal Structure of Protein FN1578 from Fusobacterium nucleatum. Northeast… · 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
- Elsewhere: RCSB PDB 2GSL · PDBe 2GSL
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