MolNFT v1 · #33818 · protein
Crystal structure of a conserved hypothetical protein from thermus thermophilus HB8
2CW5 · Bacterial fluorinating enzyme homolog: “Crystal structure of a conserved hypothetical protein from thermus thermophilus HB8”. X-ray diffraction, 5 pockets (best druggability 0.71). MolNFT v1 #33818 on GenesisL1: 3D structure…
- PDB
- 2CW5
- Type
- protein
- Length
- 697 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bacterial fluorinating enzyme homolog
- UniProt
- Q5SLF5
- Pockets
- 5 · best druggability 0.71
Structure
x-ray diffraction · 3 distinct chains · 23% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bacterial fluorinating enzyme homolog | protein | 235 | 23% helix, 28% strand | Q5SLF5 |
| B | Bacterial fluorinating enzyme homolog | protein | 224 | 23% helix, 29% strand | Q5SLF5 |
| C | Bacterial fluorinating enzyme homolog | protein | 238 | 22% helix, 28% strand | Q5SLF5 |
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 654 | 0.71 | 0.78 | 52 | empty |
| 2 | 396 | 0.69 | 0.81 | 39 | empty |
| 3 | 335 | 0.69 | 0.82 | 44 | empty |
| 4 | 409 | 0.67 | 0.80 | 58 | empty |
| 5 | 120 | 0.43 | 0.77 | 28 | empty |
Interfaces
3 interfaces between chains.
- A–C · 1393 Ų buried · 17 hydrogen bonds · protein-protein
- A–B · 980 Ų buried · 7 hydrogen bonds · protein-protein
- B–C · 813 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified (engineered).
Compared structures
- 2CW5 · Crystal structure of a conserved hypothetical protein from Thermus thermophilus HB8 · 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 Q5SLF5
- Elsewhere: RCSB PDB 2CW5 · PDBe 2CW5 · UniProt Q5SLF5
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