Research workbench
Crystal structure of T4 protein spackle as determined by native sad phasing
Analyse Crystal structure of T4 protein spackle as determined by native sad phasing in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6X6O
- Type
- protein
- Length
- 149 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein spackle
- UniProt
- P39230
- Ligands
- CL
Structure
x-ray diffraction · 2 distinct chains · 77% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein spackle | protein | 73 | 79% helix, 3% strand | P39230 |
| B | Protein spackle | protein | 76 | 75% helix, 3% strand | P39230 |
Ligands and binding sites
- CL · Chloride ion · ion · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 507 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 6X6O · Crystal structure of T4 protein Spackle as determined by native SAD phasing · 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 P39230
- Elsewhere: RCSB PDB 6X6O · PDBe 6X6O · UniProt P39230
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