Research workbench
Structure of the amyloid-forming segment tiitle from P53 (residues 253-258)
Analyse Structure of the amyloid-forming segment tiitle from P53 (residues 253-258) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4RP7
- Type
- protein
- Length
- 6 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tiitle hexapeptide segment from P53
- UniProt
- P04637
- Ligands
- ZN
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| Z | Tiitle hexapeptide segment from P53 | protein | 6 | 0% helix, 0% strand | P04637 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains Z
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 4RP7 · Structure of the amyloid-forming segment TIITLE from p53 (residues 253-258) · 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 4RP7 · PDBe 4RP7 · UniProt P04637
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