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High resolution solution NMR structure of the oligomerization domain of P53 by multi-dimensional NMR (sac structures)
Analyse High resolution solution NMR structure of the oligomerization domain of P53 by… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SAK
- Type
- protein
- Length
- 168 residues
- Chains
- 4
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tumor suppressor P53
- UniProt
- P04637
Structure
solution nmr · 1 distinct chain · 50% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Tumor suppressor P53 | protein | 42 | 50% helix, 17% strand | P04637 |
Interfaces
6 interfaces between chains.
- A–C · 1220 Ų buried · 18 hydrogen bonds · protein-protein
- B–D · 1213 Ų buried · 18 hydrogen bonds · protein-protein
- C–D · 447 Ų buried · 0 hydrogen bonds · protein-protein
- A–B · 445 Ų buried · 0 hydrogen bonds · protein-protein
- A–D · 126 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 1SAK · High resolution solution NMR structure of the oligomerization domain of P53 by… · 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
- Every structure of UniProt P04637
- Elsewhere: RCSB PDB 1SAK · PDBe 1SAK · UniProt P04637
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