Research workbench
Crystal structure of the R185A mutant of the N-terminal domain of the group B streptococcus alpha C protein
Analyse Crystal structure of the R185A mutant of the N-terminal domain of the group B… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2O0I
- 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 · 37% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| 1 | C protein alpha-antigen | protein | 180 | 37% helix, 28% strand | Q02192 |
Compared structures
- 2O0I · crystal structure of the R185A mutant of the N-terminal domain of the Group B… · the same entry in another collection · chain 1 against 1, TM-score 1.00
- Q02192 · AlphaFold monomer V2.0 prediction for C protein alpha-antigen (Q02192) · a predicted model of the same protein · chain 1 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 2O0I · PDBe 2O0I · UniProt Q02192
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