Research workbench
Structure of the major pilin protein (T-13) from streptococcus pyogenes serotype GAS131465
Analyse Structure of the major pilin protein (T-13) from streptococcus pyogenes… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6BBT
- Type
- protein
- Length
- 531 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Major pilin backbone protein T-antigen, T13
- UniProt
- A0A096ZHE3
- Ligands
- CA, CL
- Pockets
- 2 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 1% helix, 55% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Major pilin backbone protein T-antigen, T13 | protein | 264 | 1% helix, 56% strand | A0A096ZHE3 |
| B | Major pilin backbone protein T-antigen, T13 | protein | 267 | 1% helix, 54% strand | A0A096ZHE3 |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains A, B
- CL · Chloride ion · ion · chains B
- GOL · Glycerol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 936 | 0.74 | 0.77 | 86 | empty |
| 2 | 255 | 0.55 | 0.77 | 32 | empty |
Interfaces
1 interface between chains.
- A–B · 884 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 isopeptide (isopeptide).
Compared structures
- 6BBT · Structure of the major pilin protein (T-13) from Streptococcus pyogenes serotype GAS131465 · 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 A0A096ZHE3
- Elsewhere: RCSB PDB 6BBT · PDBe 6BBT · UniProt A0A096ZHE3
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