Research workbench
Streptococcus agalactiae AGI/II polypeptide bspa C terminal domain (wt)
Analyse Streptococcus agalactiae AGI/II polypeptide bspa C terminal domain (wt) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5DZA
- Type
- protein
- Length
- 312 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bspa
- UniProt
- Q8E589
- Pockets
- 2 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 8% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bspa | protein | 312 | 8% helix, 50% strand | Q8E589 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 2 copies · chains A
- PEG · Di(hydroxyethyl)ether · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 148 | 0.51 | 0.79 | 19 | EDO, PEG |
| 2 | 62 | 0.28 | 0.74 | 21 | empty |
Modifications
Observed in the structure: 2 isopeptide (isopeptide).
Compared structures
- 5DZA · Streptococcus agalactiae AgI/II polypeptide BspA C terminal domain (WT) · 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 Q8E589
- Elsewhere: RCSB PDB 5DZA · PDBe 5DZA · UniProt Q8E589
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