Research workbench
Crystal structure of the N-terminal domain of group B streptococcus alpha C protein
Analyse Crystal structure of the N-terminal domain of group B streptococcus alpha C… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1YWM
- Type
- protein
- Length
- 180 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- C protein alpha-antigen
- UniProt
- Q02192
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | C protein alpha-antigen | protein | 180 | 38% helix, 27% strand | Q02192 |
Ligands and binding sites
- GOL · Glycerol · additive · 2 copies · chains A
- DTU · (2R,3S)-1,4-dimercaptobutane-2,3-diol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1YWM · Crystal structure of the N-terminal domain of group B Streptococcus alpha C protein · the same entry in another collection · chain A against A, TM-score 1.00
- Q02192 · AlphaFold monomer V2.0 prediction for C protein alpha-antigen (Q02192) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 Q02192
- Elsewhere: RCSB PDB 1YWM · PDBe 1YWM · UniProt Q02192
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