Research workbench
Structure of the C-terminal domain of the streptococcus pyogenes antigen I/II-family protein aspa
Analyse Structure of the C-terminal domain of the streptococcus pyogenes antigen… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4OFQ
- Type
- protein
- Length
- 672 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative cell surface protein
- UniProt
- Q48S75
- Ligands
- CA
- Pockets
- 7 · best druggability 0.67
Structure
x-ray diffraction · 2 distinct chains · 11% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative cell surface protein | protein | 337 | 11% helix, 47% strand | Q48S75 |
| B | Putative cell surface protein | protein | 335 | 11% helix, 47% strand | Q48S75 |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 452 | 0.67 | 0.79 | 46 | empty |
| 2 | 548 | 0.66 | 0.77 | 57 | empty |
| 3 | 124 | 0.44 | 0.77 | 19 | empty |
| 4 | 110 | 0.38 | 0.75 | 22 | empty |
| 5 | 83 | 0.34 | 0.74 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 788 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 isopeptide (isopeptide).
Compared structures
- 4OFQ · Structure of the C-terminal domain of the Streptococcus pyogenes antigen I/II-family… · 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 Q48S75
- Elsewhere: RCSB PDB 4OFQ · PDBe 4OFQ · UniProt Q48S75
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