Research workbench
Crystal structure of the thermus thermophilus hypothetical protein TTHA0967, a thioesterase superfamily member
Analyse Crystal structure of the thermus thermophilus hypothetical protein TTHA0967, a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2CWZ
- Type
- protein
- Length
- 549 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thioesterase family protein
- UniProt
- Q5SJP1
- Pockets
- 6 · best druggability 0.68
Structure
x-ray diffraction · 2 distinct chains · 27% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thioesterase family protein | protein | 138 | 25% helix, 47% strand | Q5SJP1 |
| B, C, D | Thioesterase family protein | protein | 137 | 28% helix, 47% strand | Q5SJP1 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 6 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 164 | 0.68 | 0.87 | 30 | EDO |
| 2 | 183 | 0.65 | 0.85 | 36 | empty |
| 3 | 170 | 0.65 | 0.85 | 35 | empty |
| 4 | 201 | 0.62 | 0.83 | 36 | empty |
| 5 | 76 | 0.42 | 0.80 | 12 | EDO |
Interfaces
3 interfaces between chains.
- C–D · 2279 Ų buried · 32 hydrogen bonds · protein-protein
- A–B · 2279 Ų buried · 32 hydrogen bonds · protein-protein
- A–D · 135 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 20 modified (engineered).
Compared structures
- 2CWZ · Crystal structure of the Thermus thermophilus hypothetical protein TTHA0967, a… · 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 Q5SJP1
- Elsewhere: RCSB PDB 2CWZ · PDBe 2CWZ · UniProt Q5SJP1
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