Research workbench
Model of human IGA2 determined by solution scattering, curve fitting and homology modelling
Analyse Model of human IGA2 determined by solution scattering, curve fitting and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1R70
- Type
- protein
- Length
- 1,352 residues
- Chains
- 4
- Method
- solution scattering
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Human IGA2(M1) light chain; Human IGA2(M1) heavy chain
Structure
solution scattering · 2 distinct chains · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Human IGA2(M1) light chain | protein | 214 | 0% helix, 0% strand | — |
| B, D | Human IGA2(M1) heavy chain | protein | 462 | 0% helix, 0% strand | — |
Interfaces
3 interfaces between chains.
- B–D · 136 Ų buried · 0 hydrogen bonds · protein-protein
- A–B · 98 Ų buried · 0 hydrogen bonds · protein-protein
- C–D · 94 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 1R70 · Model of human IgA2 determined by solution scattering, curve fitting and homology… · 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 1R70 · PDBe 1R70
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