Research workbench
Murine FAB/IGE in complex with profilin from hevea brasieliensis (hev B 8)
Analyse Murine FAB/IGE in complex with profilin from hevea brasieliensis (hev B 8) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7SBD
- Type
- protein
- Length
- 558 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- FAB/IGE heavy chain; FAB/IGE light chain; Profilin-2
- UniProt
- Q9STB6
- Ligands
- NAG, BMA, MAN, FUC
- Pockets
- 6 · best druggability 0.61
Structure
x-ray diffraction · 3 distinct chains · 11% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| H | FAB/IGE heavy chain | protein | 209 | 6% helix, 53% strand | — |
| L | FAB/IGE light chain | protein | 214 | 7% helix, 49% strand | — |
| C | Profilin-2 | protein | 135 | 27% helix, 30% strand | Q9STB6 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains H
- BMA · beta-D-mannopyranose · sugar
- MAN · alpha-D-mannopyranose · sugar
- FUC · alpha-L-fucopyranose · sugar · chains H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 457 | 0.61 | 0.76 | 47 | empty |
| 2 | 118 | 0.43 | 0.77 | 24 | empty |
| 3 | 58 | 0.38 | 0.80 | 17 | empty |
| 4 | 98 | 0.34 | 0.74 | 19 | empty |
| 5 | 70 | 0.32 | 0.75 | 12 | empty |
Interfaces
3 interfaces between chains.
- H–L · 1574 Ų buried · 11 hydrogen bonds · protein-protein
- L–C · 555 Ų buried · 12 hydrogen bonds · protein-protein
- H–C · 411 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 disulfide, 1 glycan (disulfide, N-glycosylation).
Compared structures
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 Q9STB6
- Elsewhere: RCSB PDB 7SBD · PDBe 7SBD · UniProt Q9STB6
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