Research workbench
Crystal structure of the sgta homodimerization domain with covalent modifications to both C38
Analyse Crystal structure of the sgta homodimerization domain with covalent… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4GOF
- Type
- protein
- Length
- 104 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Small glutamine-rich tetratricopeptide repeat-containing protein alpha
- UniProt
- O43765
- Ligands
- CL
Structure
x-ray diffraction · 1 distinct chain · 67% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Small glutamine-rich tetratricopeptide repeat-containing protein alpha | protein | 52 | 67% helix, 0% strand | O43765 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 783 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent (additive adduct).
Compared structures
- 4GOF · Crystal structure of the SGTA homodimerization domain with covalent modifications to both… · the same entry in another collection · chain A against A, TM-score 1.00
- O43765 · AlphaFold monomer V2.0 prediction for small glutamine-rich tetratricopeptide… · a predicted model of the same protein · chain A against A, TM-score 0.80
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 O43765
- Elsewhere: RCSB PDB 4GOF · PDBe 4GOF · UniProt O43765
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