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Structural differences in the DNA binding domains of human P53 and its C. elegans ortholog cep-1: structure of C. elegans cep-1
Analyse Structural differences in the DNA binding domains of human P53 and its C.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1T4W
- Type
- protein
- Length
- 196 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- C.ELEGANS P53 tumor suppressor-like transcription factor
- UniProt
- Q20646
- Ligands
- ZN
Structure
x-ray diffraction · 1 distinct chain · 17% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | C.ELEGANS P53 tumor suppressor-like transcription factor | protein | 196 | 17% helix, 39% strand | Q20646 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1T4W · Structural Differences in the DNA Binding Domains of Human p53 and its C. elegans… · the same entry in another collection · chain A against A, TM-score 1.00
- Q20646 · AlphaFold monomer V2.0 prediction for transcription factor cep-1 (Q20646) · a predicted model of the same protein · 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 Q20646
- Elsewhere: RCSB PDB 1T4W · PDBe 1T4W · UniProt Q20646
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