Research workbench
Crystal structure of the C-terminal domain of tagh
Analyse Crystal structure of the C-terminal domain of tagh in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5BND
- Type
- protein
- Length
- 537 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ABC transporter, ATP-binding protein
- UniProt
- Q5HN63
- Pockets
- 1 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 15% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | ABC transporter, ATP-binding protein | protein | 179 | 15% helix, 42% strand | Q5HN63 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 742 | 0.69 | 0.76 | 82 | empty |
Interfaces
3 interfaces between chains.
- A–B · 866 Ų buried · 9 hydrogen bonds · protein-protein
- B–C · 850 Ų buried · 9 hydrogen bonds · protein-protein
- A–C · 29 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 5BND · Crystal structure of the C-terminal domain of TagH · 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 Q5HN63
- Elsewhere: RCSB PDB 5BND · PDBe 5BND · UniProt Q5HN63
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