Research workbench
Structure of the dimerized cytoplasmic domain of P23 in solution, NMR, 10 structures
Analyse Structure of the dimerized cytoplasmic domain of P23 in solution, NMR, 10… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1P23
- Type
- protein
- Length
- 56 residues
- Chains
- 4
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transmembrane protein TMP21 precursor
- UniProt
- Q28735
- Pockets
- 1 · best druggability 0.62
Structure
solution nmr · 1 distinct chain · 79% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Transmembrane protein TMP21 precursor | protein | 14 | 79% helix, 0% strand | Q28735 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 253 | 0.62 | 0.81 | 28 | empty |
Interfaces
5 interfaces between chains.
- B–C · 299 Ų buried · 0 hydrogen bonds · protein-protein
- A–D · 290 Ų buried · 0 hydrogen bonds · protein-protein
- C–D · 170 Ų buried · 1 hydrogen bond · protein-protein
- A–B · 139 Ų buried · 0 hydrogen bonds · protein-protein
- B–D · 50 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 1P23 · Structure of the dimerized cytoplasmic domain of P23 in solution, NMR, 10 structures · the same entry in another collection · chain A against A, TM-score 1.00
- Q28735 · AlphaFold monomer V2.0 prediction for transmembrane EMP24 domain- containing protein 10… · a predicted model of the same protein · chain A against A, TM-score 0.40
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 Q28735
- Elsewhere: RCSB PDB 1P23 · PDBe 1P23 · UniProt Q28735
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