Research workbench
Hetero-tetrameric L27 (lin-2, lin-7) domain complexes as organization platforms of supra-molecular assemblies
Analyse Hetero-tetrameric L27 (lin-2, lin-7) domain complexes as organization platforms… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1RSO
- Type
- protein
- Length
- 232 residues
- Chains
- 4
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Presynaptic protein SAP97; Peripheral plasma membrane protein cask
- EC
- 2.7.1.-
- UniProt
- Q62696, Q62915
Structure
solution nmr · 2 distinct chains · 70% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Presynaptic protein SAP97 | protein | 60 | 67% helix, 8% strand | Q62696 |
| B, D | Peripheral plasma membrane protein cask (EC 2.7.1.-) | protein | 56 | 73% helix, 0% strand | Q62915 |
Interfaces
6 interfaces between chains.
- A–B · 1463 Ų buried · 7 hydrogen bonds · protein-protein
- C–D · 1340 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 542 Ų buried · 9 hydrogen bonds · protein-protein
- B–C · 365 Ų buried · 6 hydrogen bonds · protein-protein
- A–D · 357 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 1RSO · Hetero-tetrameric L27 (Lin-2, Lin-7) domain complexes as organization platforms of… · the same entry in another collection · chain D against D, TM-score 1.00
- Q62696 · AlphaFold monomer V2.0 prediction for disks large homolog 1 (Q62696) · a predicted model of the same protein · chain C against A, TM-score 0.73
- Q62915 · AlphaFold monomer V2.0 prediction for peripheral plasma membrane protein cask (Q62915) · a predicted model of the same protein · chain B against A, TM-score 0.66
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 Q62696
- Every structure of UniProt Q62915
- Elsewhere: RCSB PDB 1RSO · PDBe 1RSO · UniProt Q62696 · UniProt Q62915
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