Research workbench
Dimeric Immunoglobin A (dIgA)
Analyse Dimeric Immunoglobin A (dIgA) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7JG1
- Type
- protein
- Length
- 1,045 residues
- Chains
- 5
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.3
- Source
- Mus musculus
- Molecule
- Igh protein; Immunoglobulin J chain
- UniProt
- Q99M22, P01592
- Ligands
- NAG
- Pockets
- 9 · best druggability 0.76
Structure
electron microscopy · resolution 3.3 · 4 distinct chains · 9% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Igh protein | protein | 231 | 9% helix, 42% strand | Q99M22 |
| B | Igh protein | protein | 224 | 9% helix, 46% strand | Q99M22 |
| D | Igh protein | protein | 228 | 11% helix, 43% strand | Q99M22 |
| J | Immunoglobulin J chain | protein | 131 | 3% helix, 47% strand | P01592 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains J, A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 756 | 0.76 | 0.81 | 68 | empty |
| 2 | 791 | 0.76 | 0.80 | 69 | empty |
| 3 | 94 | 0.50 | 0.82 | 17 | empty |
| 4 | 100 | 0.46 | 0.80 | 21 | empty |
| 5 | 138 | 0.45 | 0.76 | 22 | empty |
Interfaces
10 interfaces between chains.
- C–D · 2035 Ų buried · 21 hydrogen bonds · protein-protein
- C–J · 1949 Ų buried · 27 hydrogen bonds · protein-protein
- A–J · 1896 Ų buried · 21 hydrogen bonds · protein-protein
- A–B · 1786 Ų buried · 14 hydrogen bonds · protein-protein
- A–C · 489 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 19 disulfide, 4 glycan (disulfide, N-glycosylation, O-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 Q99M22
- Every structure of UniProt P01592
- Elsewhere: RCSB PDB 7JG1 · PDBe 7JG1 · UniProt Q99M22 · UniProt P01592
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