Research workbench
Structure of the amyloid-forming segment ltiitle from P53 (residues 252-258)
Analyse Structure of the amyloid-forming segment ltiitle from P53 (residues 252-258) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4RP6
- Type
- protein
- Length
- 7 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ltiitle heptapeptide segment from P53
- UniProt
- P04637
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| Z | Ltiitle heptapeptide segment from P53 | protein | 7 | 0% helix, 0% strand | P04637 |
Compared structures
- 4RP6 · Structure of the amyloid-forming segment LTIITLE from p53 (residues 252-258) · the same entry in another collection · chain Z against Z, 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 4RP6 · PDBe 4RP6 · UniProt P04637
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