Research workbench
Type IV-like pilin TTHA1219 from thermus thermophilus
Analyse Type IV-like pilin TTHA1219 from thermus thermophilus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5G23
- Type
- protein
- Length
- 770 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Type-IV like pilin TTHA1219
- UniProt
- Q5SIZ5
- Pockets
- 6 · best druggability 0.79
Structure
x-ray diffraction · 4 distinct chains · 13% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Type-IV like pilin TTHA1219 | protein | 191 | 11% helix, 42% strand | Q5SIZ5 |
| B | Type-IV like pilin TTHA1219 | protein | 194 | 15% helix, 42% strand | Q5SIZ5 |
| C | Type-IV like pilin TTHA1219 | protein | 191 | 13% helix, 42% strand | Q5SIZ5 |
| D | Type-IV like pilin TTHA1219 | protein | 194 | 13% helix, 40% strand | Q5SIZ5 |
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 960 | 0.79 | 0.81 | 107 | empty |
| 2 | 331 | 0.64 | 0.79 | 32 | empty |
| 3 | 304 | 0.61 | 0.78 | 35 | empty |
| 4 | 134 | 0.49 | 0.79 | 25 | empty |
| 5 | 87 | 0.38 | 0.77 | 19 | empty |
Interfaces
5 interfaces between chains.
- C–D · 1588 Ų buried · 17 hydrogen bonds · protein-protein
- A–B · 1543 Ų buried · 13 hydrogen bonds · protein-protein
- B–C · 407 Ų buried · 1 hydrogen bond · protein-protein
- A–D · 381 Ų buried · 4 hydrogen bonds · protein-protein
- B–D · 301 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
Compared structures
- 5G23 · Type IV-like pilin TTHA1219 from Thermus thermophilus · 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 Q5SIZ5
- Elsewhere: RCSB PDB 5G23 · PDBe 5G23 · UniProt Q5SIZ5
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