MolNFT v1 · #33753 · protein
Crystal structure of TT1568 from thermus thermophilus HB8
2CU3 · Unknown function protein: “Crystal structure of TT1568 from thermus thermophilus HB8”. X-ray diffraction, 1 ligand (CD), 1 pocket (best druggability 0.57). MolNFT v1 #33753 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 2CU3
- Type
- protein
- Length
- 127 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Unknown function protein
- UniProt
- Q72KL7
- Ligands
- CD
- Pockets
- 1 · best druggability 0.57
Structure
x-ray diffraction · 2 distinct chains · 22% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Unknown function protein | protein | 63 | 22% helix, 35% strand | Q72KL7 |
| B | Unknown function protein | protein | 64 | 22% helix, 34% strand | Q72KL7 |
Ligands and binding sites
- CD · Cadmium ion · metal · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 293 | 0.57 | 0.77 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 398 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified (engineered).
Compared structures
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 Q72KL7
- Elsewhere: RCSB PDB 2CU3 · PDBe 2CU3 · UniProt Q72KL7
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