Research workbench
N-terminal DNA binding domain of the antitoxin phd from phage P1
Analyse N-terminal DNA binding domain of the antitoxin phd from phage P1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4ZLX
- Type
- protein
- Length
- 94 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Antitoxin phd
- UniProt
- Q06253
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Antitoxin phd | protein | 47 | 47% helix, 36% strand | Q06253 |
Ligands and binding sites
- ACT · Acetate ion · additive · 5 copies · chains B, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 1311 Ų buried · 24 hydrogen bonds · protein-protein
Compared structures
- 4ZLX · N-terminal DNA binding domain of the antitoxin Phd from phage P1 · 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 Q06253
- Elsewhere: RCSB PDB 4ZLX · PDBe 4ZLX · UniProt Q06253
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