Research workbench
Crystal structure of the tgs domain of the CLOLEP_03100 protein from clostridium leptum, northeast structural genomics consortium target QLR13A
Analyse Crystal structure of the tgs domain of the CLOLEP_03100 protein from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3HVZ
- Type
- protein
- Length
- 382 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized protein
- UniProt
- A7VWX7
- Pockets
- 2 · best druggability 0.36
Structure
x-ray diffraction · 2 distinct chains · 21% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, F | Uncharacterized protein | protein | 64 | 20% helix, 42% strand | A7VWX7 |
| E | Uncharacterized protein | protein | 62 | 21% helix, 37% strand | A7VWX7 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 126 | 0.36 | 0.72 | 24 | empty |
| 2 | 64 | 0.29 | 0.73 | 18 | empty |
Interfaces
6 interfaces between chains.
- C–D · 707 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 664 Ų buried · 9 hydrogen bonds · protein-protein
- E–F · 648 Ų buried · 5 hydrogen bonds · protein-protein
- A–D · 382 Ų buried · 2 hydrogen bonds · protein-protein
- C–F · 363 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 6 modified (engineered).
Compared structures
- 3HVZ · Crystal Structure of the TGS domain of the CLOLEP_03100 protein from Clostridium leptum… · 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 A7VWX7
- Elsewhere: RCSB PDB 3HVZ · PDBe 3HVZ · UniProt A7VWX7
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