Research workbench
Type IV-like pilin TTHA1218 from thermus thermophilus
Analyse Type IV-like pilin TTHA1218 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
- 5G25
- Type
- protein
- Length
- 82 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Type-IV like competence pilin TTHA1218
- UniProt
- Q5SIZ6
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Type-IV like competence pilin TTHA1218 | protein | 82 | 26% helix, 43% strand | Q5SIZ6 |
Ligands and binding sites
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 5G25 · Type IV-like pilin TTHA1218 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 Q5SIZ6
- Elsewhere: RCSB PDB 5G25 · PDBe 5G25 · UniProt Q5SIZ6
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